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Light Microscopy Interest Group
A mission of The Light Microscopy Special Interest Group (LMIG) is to inform the NIH community about cutting-edge research in light fluorescence microscopy and about available resources, both extramural and intramural. LMIG aims to build a bridge between NIH biologists and microscopists.
The Light Microscopy Special Interest Group holds monthly seminars, maintains this website and a listserv for researchers interested in light microscopy.
LMIG seminar is a NIH seminar on innovative microscopy techniques and their application to biomedical research with a focus on single-cell imaging and in-situ biophysics. The target audience is a group of researchers who are interested in microscopy and who are aware of the potential of image analysis and in vivo biophysics. The aim is to demonstrate applicability of the state-of-the art microscopy to tissue and cell biology problems. Presentations should include biological data and in-depth description of appropriate microscopy techniques. Speakers are encouraged to talk about how the technique worked in their hands including failures.
The interest group listserv may be used for discussions of microscopy problems/questions, and equipment advice.
The group moderators are Tatiana Karpova (NCI), Christian Combs (NHLBI) and Ulrike Boehm (NCI).
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Date and Location:
Tuesday, October 16, 2018; 11 am, 37 Convent Drive, Bethesda MD 20892; NIH, Bldg 37/ Rm 4107/4041 (fourth floor)
Speaker: Dr. Kyung Lee (NIH/NCI)
Title: "Structure and Function of Mammalian Centrosomal Assemblies."
As the main microtubule-organizing center for animal cells, centrosomes are critically required for various cellular processes, including bipolar spindle formation and mitotic chromosome segregation. They are composed of two orthogonally arranged centrioles, which duplicate early in the cell cycle in a manner that takes place only once per each cycle. Accurate control of centriole numbers is essential for normal chromosome segregation and maintenance of genomic integrity. A growing body of evidence suggests that mammalian polo-like kinase 4 (Plk4) plays a key role in inducing centriole duplication. Plk4 localizes to distinct subcentrosomal sites by interacting with a centrosomal scaffold protein, Cep152. Interestingly, Cep152 tightly binds to another scaffold protein, Cep63, and this step appears to be critical to assemble a higher-order cylindrical architecture around a centriole. Notably, mutations in the Cep152 and Cep63 scaffolds are frequently linked to various human diseases, such as cancer, microcephaly, ciliopathy, and dwarfism. Therefore, investigating the molecular basis of how these scaffolds are assembled into a higher-order structure and how the assembled architecture promotes Plk4-dependent centriole duplication will be important not only to understand one of the most fundamental cellular processes of centrosomal organization but also to discover the causes of human genetic disorders associated with centrosome abnormalities. Our latest findings on the molecular nature and biological significance of the Cep152•Cep63 complex-generated cylindrical self-assembly will be discussed.
 Lawo, S., Hasegan, M., Gupta, G. D. & Pelletier, L. Subdiffraction imaging of centrosomes reveals higher-order organizational features of pericentriolar material. Nat. Cell Biol. 14, 1148-1158. (2012).
 Park, S. Y. et al. Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. Nat. Struct. Mol. Biol. 21, 696-703, doi:10.1038/nsmb.2846 (2014).
Building 37, conference room (4107/4041)
Feel free to download the 2018 seminar schedule here
Seminars in 2018
Tuesday, September 18, 2018
Dr. Mihaela Serpe (NIH/NICHD) "Molecular mechanisms of synapse assembly and homeostasis – lessons from genetics and imaging in flies."
The purpose of our research is to understand the mechanisms of synapse development and homeostasis. Using the Drosophila neuromuscular junction (NMJ) as a model for glutamatergic synapse, we focus on three key processes in synaptogenesis: (1) trafficking of components to the proper site, (2) organizing those components to build synaptic structures, and (3) maturation and homeostasis of the synapse to optimize its activity. We address the mechanisms underlying these processes using a comprehensive set of approaches including genetics, biochemistry, molecular biology, super resolution imaging and electrophysiology recordings in live animals and reconstituted systems. I will emphasize how microscopy techniques have enabled our recent accomplishments: (1) identification of a key auxiliary protein of glutamatergic synapses, called Neto, that is essential for their development and function both in Drosophila and mammals, and the molecular dissection of its activities, and (2) analysis of the action of the TGF-β pathway in synaptic plasticity, and in particular the discovery of a novel mechanism by which local, non-transcriptional BMP signaling directly modulates synapse structure and activity.
Tuesday, May 15, 2018
Dr. Philip Anfinrud (NIH/NIDDK) "Watching proteins function in real time via picosecond X-ray diffraction."
To understand how a protein functions, it is crucial to know the time-ordered sequence of structural changes associated with its function. To that end, we have developed numerous experimental techniques for characterizing structural changes in proteins over time scales ranging from femtoseconds to seconds. This talk will focus primarily on time-resolved X-ray studies performed on the BioCARS beamline at the Advanced Photon Source, which allowed us to characterize structural changes in proteins with 150-ps time resolution. We have used this capability to track the reversible photocycle of photoactive yellow protein following trans-to-cis photoisomerization of its p-coumaric acid (pCA) chromophore. Briefly, a picosecond laser pulse photoexcites pCA and triggers a structural change in the protein, which is probed with a suitably delayed picosecond X-ray pulse. When the protein is studied in a crystalline state, this “pump-probe” approach recovers time-resolved diffraction “snapshots” whose corresponding electron density maps can be stitched together into a real-time movie of the structural changes that ensue. However, the actual signaling state is not accessible in the crystalline state due to crystal packing constraints. This state is accessible in time-resolved small- and wide-angle X-ray scattering studies, which probe changes in the size, shape, and structure of the protein. These studies help provide a framework for understanding protein function, and for assessing and validating theoretical/computational approaches in protein biophysics . This research was supported in part by the Intramural Research Program of the NIH, NIDDK.
Tuesday, April 17, 2018
Simona Patange (NIH/NCI) "A living, single cell view of MYC's effects on transcription."
How does a transcription factor transmit information to a gene in a single cell context? To answer this question we examine the oncogenic transcription factor c-MYC. MYC is upregulated in most human cancers, yielding a global increase in gene expression. However the mechanism by which MYC amplifies transcription, and why it promotes cancer, has remained notoriously elusive. To address this gap in understanding we seek a quantitative, single-cell view of how MYC modulates the kinetics of transcription. We use two recently-developed imaging techniques: 1) single-molecule FISH to quantify RNA in fixed cells, and 2) live cell imaging of transcription with the MS2-PP7 stem loop system to observe real-time RNA production at a given gene locus. We predict that if MYC amplifies gene expression, then we would observe either an increase in the frequency of transcription events, or the duration of transcription events, or a combination of the two. Our results looking at the effect of MYC perturbations on both an exogenous reporter and endogenous gene show that MYC increases the duration of transcription events— this results in greater gene expression, but also an increase in its heterogeneity. These findings provide living, single cell evidence of MYC as a global amplifier of gene expression and suggests that the mechanism is by stabilizing the active period of a gene. We speculate that the added consequence of MYC’s propensity to increase gene expression heterogeneity could drive cells to transiently populate pathological states and phenotypes that may ultimately make them susceptible to cancer.
Tuesday, March 20, 2018
Dr. Jie Xiao (Johns Hopkins U Sch Med) "Quantitative superresolution imaging for bacterial cell biology"
Single-molecule localization based superresolution microscopy (SMLM) not only can reveal fine dimensional details of cellular structures beyond the diffraction limit, but also can provide lists of molecular coordinates to enable the critical ability of quantifying the number, clustering, complexity, colocalization and organization of biomolecules with 10-50 nm resolution. When coupled with genetic and biochemical investigations, these methods are powerful in accessing new information not possible before. In this talk I will discuss a few case studies in which SMLM allows us to understand the assembly, organization, function and dynamics of a variety of bacterial cellular structures.
Tuesday, January 16, 2018
Dr. Matthew Wooten (Johns Hopkins U Sch Med) "Super Resolution as a tool to study a potential role for DNA replication in establishing distinct epigenomes"
The primary function of DNA replication is to duplicate the genome. However, the process of DNA replication must also duplicate epigenetic information. Epigenetic mechanisms play a key role in altering chromatin structure and gene expression patterns, and in specifying and maintaining stem cell identity throughout cell division. Many types of stem cells have the ability to asymmetrically divide to give rise to one daughter cell capable of self-renewal and another daughter capable of differentiating. Using a dual-color labeling system, we demonstrated that in the Drosophila germline H3 is inherited asymmetrically whereas the H3 variant H3.3 is inherited symmetrically. As H3 is incorporated during S-phase whereas H3.3 is incorporated in a replication-independent manner, we hypothesize that old and new H3 are differentially incorporated into distinct sister chromatids during DNA replication. Because the average diameter of replication forks in eukaryotic cells (~150 - 400 nm) is at or below the diffraction-limited resolution of conventional fluorescence light microscopy (250 - 300 nm), we used single molecule localization based super-resolution (SR) imaging to examine the spatial distribution of old and new H3 and H3.3 in interphase GSCs. Interestingly, we were able to observe that these two histone species show significantly different co-localization patterns throughout interphase. We have developed a method using STED SR microscopy in tandem with the chromatin fiber technique to observe asymmetries in DNA replication as well as unique patterns in the distribution of H3 versus H3.3 in newly replicated sister chromatids. H3-labeled chromatin fibers show a significantly higher degree of asymmetry than do H3.3 chromatin fibers, which may be a basis for the distinct patterns of H3 and H3.3 inheritance at the genome-wide level. In addition, during replication-coupled nucleosome assembly, old histones preferentially associate with the leading strand whereas new histones preferentially associate with the lagging strand. Based on these data, we propose that the asymmetries inherent to the process of DNA replication serve to bias histone inheritance such that the leading strand preferentially inherits old histone and the lagging strand preferentially inherits new histones.
Seminars in 2017
Tuesday, December 12, 2017
Dr. Ulrike Boehm (NIH/NCI) "4Pi‐RESOLFT nanoscopy: Nanometer scale 3D fluorescence imaging in whole living cells"
By enlarging the aperture along the optic axis, the coherent utilization of opposing objective lenses (4Pi arrangement) has the potential to offer the sharpest and most light-efficient point-spread-functions in three-dimensional (3D) far-field fluorescence nanoscopy. However, to obtain unambiguous images, the signal has to be discriminated against contributions from lobes above and below the focal plane, which has tentatively limited 4Pi arrangements to imaging samples with controllable optical conditions. Here I apply the 4Pi scheme to RESOLFT nanoscopy using two-photon absorption for the on-switching of reversibly switchable fluorescent proteins (RSFPs). I show that in this combination, the lobes are so low that low-light level, 3D nanoscale imaging of living cells becomes possible. This method thus offers robust access to densely packed, axially extended cellular regions that have been notoriously difficult to super-resolve. This approach also entails a fluorescence read-out scheme that translates molecular sensitivity to local off-switching rates into improved signal-to-noise ratio and resolution. In conclusion, by realizing 4Pi-RESOLFT nanoscopy based on RSFPs, I demonstrate exceptional optical sectioning in coordinate-targeted far-field fluorescence nanoscopy, which greatly facilitates nanometer scale 3D fluorescence imaging in living cells.
Tuesday, November 14, 2017
Dr. Kandice Tanner (NIH/NCI) "Probing the physical properties of the microenvironment in vivo"
Tissue is composed of heterogeneous biological components that modulate physical properties within the microenvironment. Transformation of the physico-chemical properties of the stromal microenvironment such as changes in the extracellular matrix (ECM) has been shown to be associated with cancer progression. Cells respond to both chemical and physical cues of the microenvironment. In tissue, chemical and mechanical cues are both modulated by changes in ligand density and localized tissue architecture. Hence, decoupling chemical cues from those due to the physical changes is non-trivial. What is needed is the ability to resolve and quantitate minute forces that cells sense in the local environment (on the order of microns) within thick tissue (in mm). To achieve this, we employ a method to quantitate absolute tissue mechanics using in vitro and in vivo models. We performed Active Microrheology by optical trapping in vivo, using in situ calibration to accurately apply and measure forces. With micrometer resolution at broadband frequencies and depths approaching 0.5 mm, we probed differential stresses and strains on force, time and length scales relevant to cellular processes in living zebrafish. We determined that proxy calibration methods overestimate complex moduli by as much as ~20 fold. While ECM hydrogels displayed rheological properties predicted for polymer networks, new models may be needed to describe the behavior of tissues observed. Finally, we validated our in vitro findings in an in vivo model using zebrafish as our model for metastasis. We believe that this platform can be used in elucidating the basic mechanisms that govern the role of material properties in mechanobiology.
Tuesday, October 17, 2017
Dr. Petr Kalab (Johns Hopkins U) "Fluorescence lifetime imaging microscopy (FLIM) for quantitative live-cell measurements with Forster resonance energy transfer (FRET) probes"
Most of the commonly used fluorescence microscopy techniques today depend on the detection of the emission intensity of various fluorescent proteins, dyes or endogenous reports. In addition to the crucially useful separation of the emission and excitation wavelengths, the fluorescence process offers another exciting and so far underused opportunity to explore living cells through the fluorescence lifetimes of fluorophores. The fluorescence lifetime, which is independent of the emission intensity, is a measure of the time it takes before the excited fluorophore returns to its ground state. The interesting feature of fluorescence is that the energy dissipation from the excited state depends on the molecular condition of the fluorophores (protonation, oxygenation, etc.) and their environment (such as binding to fluorescent or non-fluorescent molecules). Because of that, the fluorescence lifetime imaging microscopy (FLIM) has the potential to provide real-time measurements of molecular interactions and biochemical reactions in live cells. The time-correlated single photon counting (TCSPC) method of FLIM provides better lifetime resolution and higher photon usage efficiency than its main alternative, the fluorescence polarization FLIM. We used the TCSPC FLIM with monomolecular FRET reporters to study the role of the small GTPase Ran in the regulation of mitosis, cell cycle or DNA repair. In those studies, the quantitative properties of the FLIM/FRET imaging gave us the particularly useful insights. FLIM provides a rigorous and quantitative method of FRET measurements and has several distinct advantages over the intensity-based methods, including relaxed concerns for spectral crosstalks (only donor emission is detected), insensitivity to sensor concentration (within reasonable limits) and the straightforward relationship between the measured lifetimes and FRET efficiency. The main limitations in FLIM/FRET, which should not be underestimated, is the need for a large number of photons (about 1000/bin) to resolve 2-3 exponential lifetimes that are typical for all fluorophores in the cellular environment. While the technology is constantly evolving, the application of FLIM/FRET requires careful consideration of the necessary temporal or spatial resolution. In this presentation, I will provide a brief overview of the main theoretical and namely practical aspects of FRET detection with FLIM. These topics will include the design of FRET sensors for FLIM, the important features of excitation sources and detectors, and the available FLIM computation methods, including the global analysis via the Phasor approach. Finally, since some of the data that I will discuss we acquired with the still fully functional equipment in the NCI imaging core, the talk could serve as an introduction to the users of the facility who are interested in applying FLIM in their research.
Tuesday, September 19, 2017
Dr. Steven S Vogel (NIH/NIAAA) "Ultra-Fast Long-Distance Energy Transfer Between Fluorescent Proteins"
An implicit and often unmentioned assumption of studies utilizing genetically encoded Green Fluorescent Protein, its derivatives, and structurally related fluorescent proteins (FPs), is that they behave like classical organic fluorophores. When conventional fluorophores are in close-proximity (< 1 nm) and/or are cooled to temperatures approaching absolute zero, coherent energy transfer (CET) may enable multiple fluorophores to behave as a single quantum entity. CET is thought to play a key role in photosynthesis, and vis-à-vis technology, may enable quantum computing. CET can manifest as ultra-fast long-distance energy transfer within fluorophore assemblies. Antibunching and Davydov splitting of circular dichroism (CD) spectra, uniquely quantum mechanical behaviors, are indicative of CET. Physiological temperatures extinguish CET by promoting rapid collisional dephasing of fluorophore vibrational modes (typically within 100 fs of photoexcitation). Moreover, because FP fluorophores are encased in a ß-barrel structure, proximities closer than 2 nm are not possible. Thus, CET between FPs at physiological temperatures is thought to be impossible. Nonetheless, time-resolved fluorescence anisotropy, fluorescence correlation spectroscopy, antibunching, and CD all indicate stronger than expected coupling between FPs. Paired-pulse correlation spectroscopy revealed that dephasing between coupled FPs occurs between 400-600 fs after photoexcitation, suggesting that the FP ß-barrel attenuates dephasing to allow CET.
Tuesday, June 20, 2017
Dr. Ronald N. Germain (NIH/NIAID) "Imaging Immunity – Developing a Spatiotemporal Understanding of Host Defense Using Intravital Dynamic and Multiplex Static Microscopy"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar of Dr. Ronald Germain (NIH/NIAID) about two-photon dynamic intravital and static 3D tissue imaging. For the latter Dr. Germain perfected clarification techniques and developed software that allows quantitative multichannel analysis of cellular distribution in 3D in whole organs. In combination, these two techniques lead to deep understanding of how the tissues are organized, and how this organization is dynamically maintained and adapted to microenvironment. Stunning work, stunning resource!
Tuesday, May 16, 2017
Dr. Vinay Swaminathan (NIH/NHLBI) "Co-alignment and orientation of activated integrins in focal adhesions of migrating cells studied by fluorescence polarization"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar of Dr. Vinay Swaminathan (NIH/NHLBI) about dynamic integrin response to physical and chemical information. Techniques of fluorescence polarization microscopy led to amazing discovery: integrins come to attention (co-align) obeying the trumpet of directional mechanical force. Come to this seminar to learn whether measurements of molecular anisotropy are applicable to your favorite biological system.
Tuesday, April 18, 2017
Dr. Ville Paakinaho (NIH/NCI) "Single-Molecule Imaging and the future of simultaneous tracking of Multiple Transcription Factors"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar of Dr. Ville Paakinaho (NIH/NCI) about real-time dynamics of Transcription Factor action studied by the state-of-the-art Single Molecule Tracking. In these pioneer studies Glucocorticoid Receptor (GR) and other TF were tagged with HaloTag and SNAP-tag and observed on custom-built microscope with a special illumination technique (HILO). Don't miss this presentation about the exciting new technique! Isn't it surprising how dynamic the life of the cellular molecules is?
Tuesday, March 21, 2017
Dr. Lakshmi Balagopalan (NIH/NCI) "Oh The Places LAT Goes!"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar of Dr. Lakshmi Balagopalan (NIH/NCI) about the mechanism of microcluster formation in activated T-cells. This is an excellent example of the application of cutting-edge high-resolution microscopy for kinetics of T-cell vesicle formation (Lattice LSM and TIRF-SIM). Where Biochemistry makes educated guesses, Microscopy observes!
Tuesday, January 17, 2017
Dr. Elisabeth Finn (NIH/NCI) "Examining genome-wide patterns of DNA:DNA interaction via high throughput imaging"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar of Dr. Elisabeth FInn (NIH/NCI) about genome organization and its cell-to-cell variation revealed by high-throughput FISH.
Seminars in 2016
Tuesday, November 22, 2016
Dr. Martin Schnermann (NIH/NCI) "Near IR uncaging chemistry: discovery and applications" Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about a new antibody-based drug-delivery method, based on "uncaging" of biologically active molecules by near-IR light. The use of tissue penetrant near-IR wavelengths enables in vivo applications. Dr. Schnermann (NCI) applied chemical remodeling to cyanines and developed novel cyanine fluorophores with improved properties for drug uncaging, in vivo optical imaging, and super resolution microscopy. Amazing resource!
Tuesday, October 18, 2016
Dr. Luke Lavis (HHMI, Janelia Farms) "Building brighter dyes for single-molecule imaging"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about fantastic advancements in the field of labeling live proteins in situ. Reseach of Dr. Lavis opened a new era in live imaging by permitting bright, stable and reliable labeling of protein fusions to Halo Tag, SNAP tag and CLIP tag. Single-molecule imaging is made possible by this technological achievement. Ladies and Gentlemen, PhD and MD, please greet our future Nobel laureate!
Tuesday, September 20, 2016
Dr. Jason Yi (NIH/NCI) "madSTORM: a super resolution technique for large-scale multiplexing at single molecule accuracy"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about madly successful superresolution strategy developed in CCR. madSTORM allows accurate targeting of multiple molecules using sequential binding and elution of fluorescent antibodies. madSTORM was applied to an activated T cell to localize 25 epitopes, 14 of which are on components of the same multi-molecular T cell receptor complex. Please, come! Especially if you fancy a big multisubunit complex of your own!
Tuesday, April 19, 2016
Dr. Diego Presman (NCI/NIH) "Analysis of Glucocorticoid Receptor Dynamics by Number and Brightness and Single-Molecule Tracking methods"
Can you imagine such a treat! A hunt for single molecules! Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about dynamic binding behavior and oligomerization of glucocorticoid receptors. Single molecule tracking will tell you important things about biophysical characteristics of transcriptional factors. And we want NUMBERS! Prepare yourself for a wild ride on the waves of state-of the art techniques!
Tuesday, March 22, 2016
Dr. Kenneth Jacobson (NIH/NIDDK) "Fluorescent Ligands of GPCRs: Adenosine and P2Y Receptors"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about fluorescent probes for adenosine receptors - important proteins involved in inflammation.
Tuesday, January 19, 2016
Dr. Jadranka Loncarek (NIH/NCI) "Centriole engagement: a matter of maturity?"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about super resolution, light and electron microscopy in studies of centrosome anomalies and centrosome cycle.
Seminars in 2015
Tuesday, December 15, 2015
Dr. Jan Wisniewski (Janelia Farms) "Instant 3D imaging with Multi-Focus Microscope"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about tracking of molecules in 4D made possible by innovative technique allowing simultaneous acquisition of multiple z-sections (multifocus microscopy). Until recently we had to sacrifice either speed or resolution for the low-light time-lapse fluorescent imaging, but now we may have it all and really observe individual molecules in their natural habitat.... And do some 3D PALM on the side.
Tuesday, November 18th, 2015
Dr. Dan Larson (NCI/NIH, LRBGE) "A single-molecule view of the central dogma."
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about single-molecule view on transcription. Portraits of individual mRNA will be provided, as well as info about the best hunting places for the observation of gene expression in live single cells with highest temporal and spatial resolution.
Tuesday, October 20, 2015
Dr. Christopher Westlake (NIH/NCI) "Cell antenna assembly studied by advanced fluorescence and electron microscopy imaging"
WHAT CAN Immuno Fluorescence AND Electron Microscopy TELL US ABOUT Rab SMALL GTPases? Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar on the role of Rab small GTPases and associated Rab effectors and GTPase regulators, SNAREs and membrane shaping proteins in ciliogenesis. Results are important for research in Polycystic kidney disease and other ciliopathies. This is a perfect example of how Electron and Light microscopy may be used for a structural and functional dissection of intracellular pathways.
Tuesday, September 15, 2015
Dr. Rolf Swenson (NIH/NHLBI) "The chemistry of optical imaging agents, experiences from the Imaging Probe Development Center"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar about NIH Imaging Probe Development Center (IPDC) that provides support for advanced molecular technologies. IPDC scientists can synthesize requested probes that are published in literature, but commercially unavailable, or are completely novel. They can do it for us - isn't it wonderful? And do you, personally, know that such resource is at hands distance? If not, come to this talk!
Tuesday, May 26, 2015
Dr. Sriram Subramaniam (NIH/NCI) "High resolution 3D electron microscopy: Progress and new opportunities"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar on the new vistas, cellular, of course! Now we really can do correlative Super Resolution / Electron Microscopy. And if we can, we should! Please, come to the seminar of our super-star electron and light microscopist Dr. Sriram Subramaniam, don't miss this rare opportunity!
Tuesday, May 19, 2015
Dr. Keir Neuman (NIH/NHLBI) "Background-free imaging in vivo with fluorescent nanodiamonds applied to lymph node imaging"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar on the topic of tissue imaging studied by a state-of the art fluorescent biomarkers - nanodiamonds. If you think you don't need them nanodiamonds, think again! The most important potential biological applications of fluorescent nanodiamonds include (1) biomolecular labeling, (2) cellular imaging, (3) tumor targeting, (4) single particle tracking, (5) long-term in vivo monitoring. And... nanodiamonds are within a reach for the NIH community.
Tuesday, April 21, 2015
Dr. Thomas Ried (NIH/NCI) "The NIH 4D Nucleome Initiative"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar on the topic of 4D nucleome. The NUCLEUS, naked, transparent - all the guts visible and classified, in its past, present, and future! Can we do it? We can do it!
Tuesday, March 17, 2015
Dr. Daniela Malide (NIH/NHLBI) "In vivo Clonal Tracking of Hematopoietic Stem and Progenitor Cells Marked by Five Fluorescent Proteins using Confocal and Multiphoton Microscopy"
Light Microscopy Interest Group (LMIG) organizers invite you to attend a seminar on the topic of clonal tracking of hematopoietic stem and progenitor cells studied by a genetic combinatorial marking in five shiny colors! Yes, you can track five colors!
Tuesday, January 20, 2015
Dr. Prabuddha Sengupta (NICHD/NIH, CBMB) "Mammalian plasma membrane remodeling studied by quantitative point localization microscopy"
LMIG organizers invite you to attend a seminar on the topic of HIV biogenesis studied by a state-of the art microscopy technique. Single molecule superrersolution (point localization) microscopy based data acquisition and image analysis strategies to highlight the details of the molecular mechanism of individual steps of the viral assembly process.
Seminars in 2014
Tuesday, December 16, 2014
Dr. Valentin Magidson (NCI/NIH, CCR/OD) "Insights into chromosome segregation enabled by multimodal microscopy"
Tuesday, October 14th, 2014
Dr. Jiji Chen (NCI/NIH, CCR/OD) "Single Molecule Imaging for Cellular Dynamics and Function"
Friday, November 17, 2017 – 8:50 am - 5:00 pm
Frontiers in Light Microscopy Symposium, in Bldg. 35, Conference Room 620/640 (PDF 320 KB)
June 29-30, 2017
Single Cell Analysis - 5th Annual Investigators Meeting, Masur Auditorium, NIH, Bethesda, MD (PDF 317 KB)
Monday, March 27, 2017 – 1:00-4:00 pm
CCR Building 41 Core Facilities Open House, in Bldg. 41, Conference Room C507/C509 (PDF 317 KB)
Meet the Core heads and take tours through the cores facilities
Tuesday, March 7, 2017 - 2:30-4:00 pm
NCI Core Facilities Open House, in Bldg. 35 Atrium (PDF 85 KB)
Meet with Core managers from Bldg. 37, Bldg. 41 and Frederick Cores
Please join our listserv. We use our listserv to share information about upcoming seminars. Furthermore, the listserv is open for discussions of microscopy problems/questions, equipment advice.
The direct link to join the listserv is https://list.nih.gov/cgi-bin/wa.exe?SUBED1=light_micro_interestl&A=1. Once you add your name and e-mail address, you will receive an automated e-mail message asking you to confirm your request; and then, when the Light Microscopy Interest Group moderators receive this request, you will receive confirmation that you have been added to the list.
You can leave the LIGHT_MICRO_INTERESTL listserv through the same link above.
LMIG journal club is a NIH journal club on (advanced) microscopy techniques and their application to biomedical research.
Please contact Ulrike Boehm (E-mail: email@example.com; Phone: 240.760.6581) for more information.
General Microscopy Resources
Confocal Listserv - Email discussion list focused on confocal microscopy, but also including topics on fluorescence microscopy and digital imaging.
MicroscopyU by Nikon - Online learning platform by Nikon
Leica Science Lab - Online learning platform by Leica
Microscopy Resource Center - Online learning platform by Olympus
Education in Microscopy and Digital Imaging - Online learning platform by Zeiss
Molecular Expressions - Online learning platform
iBiology Microscopy Course - Online microscopy course
Nature Milestones Light Microscopy - Collection of milestones in light microscopy
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