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Lsm 510 meta confocor3

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The LSM 510 META ConfoCor3 is a confocal laser scanning microscope system manufactured by Zeiss. It combines the capabilities of a laser scanning microscope with a fluorescence correlation spectroscopy (FCS) module, enabling advanced imaging and analysis of biological samples.

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Lab products found in correlation

Uoplan water immersion objective, by Zeiss (2 mentions) Lsm 710, by Zeiss (1 mentions) C apochromat, by Zeiss (1 mentions) Polycarbonate filter, by Avestin (1 mentions) Dope cap biotin, by Avanti Polar Lipids (1 mentions)

Close spelling variants of this product

LSM 510 (2630 citations) LSM 510 META (1974 citations) 510 Meta (155 citations) LSM 510-ConfoCor3 (2 citations)

5 protocols using lsm 510 meta confocor3

1

Confocal Imaging of Brain Slices

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LSM 510 META ConfoCor3 (Carl Zeiss) and LSM 710 (Carl Zeiss) confocal microscopes were used to image fixed brain slices. LSM 510 was used for all ex vivo imaging, except for antibody-labeled capsid samples in the cortex. For LSM 510, a 488-nm argon laser and a 561-nm diode-pumped solid-state (DPSS) laser were used to excite green fluorophores (eGFP, GCaMP6f, Alexa Fluor 488) and red fluorophores (tdTomato, TurboRFP), respectively. A 405-nm diode was used to excite DAPI. Immunostained AAV capsids in BX were imaged with LSM 710 using a 63×/NA 1.46 a-Plan-Apochromat oil objective.
Georgiou L., Echeverría A., Georgiou A, & Kuhn B. (2022). Ca+ activity maps of astrocytes tagged by axoastrocytic AAV transfer. Science Advances, 8(6), eabe5371.
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2

Fluorescence Correlation Microscopy Imaging

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Laser scanning microscopy (LSM) imaging and FCCS measurements were performed using an LSM510 META-ConfoCor3 (Carl Zeiss) equipped with a 488-nm Ar-ion laser, 543 nm He-Ne laser, and a water immersion objective (C-Apochromat, 40×, 1.2 N.A., Corr, Carl Zeiss), and avalanche photodiode detectors (APDs). eGFP and Tomato were excited using the 488-nm laser and 543-nm laser, respectively. The pinhole size was adjusted to 80 µm. The fluorescence of eGFP and Tomato was split by NFT 545. The fluorescence signal of eGFP and Tomato passed through BP505-530 (eGFP) and BP615-680 (Tomato) filter, respectively. FCCS measurements, over the cell nucleus, were carried out 10 times for a duration of 20 s each.
Oasa S., Vukojević V., Rigler R., Tsigelny I.F., Changeux J.P, & Terenius L. (2020). A strategy for designing allosteric modulators of transcription factor dimerization. Proceedings of the National Academy of Sciences of the United States of America, 117(5), 2683-2686.
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3

Covalent Labeling of Membrane Proteins

Cited 2 times
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SecYEG and GlpF were modified by site-directed mutagenesis to contain only one (SecY, A204C; periplasmic loop) or two cysteine residues (Glpf, C261and C264; both located at the periplasmic C-terminus), respectively, thereby enabling covalent labeling with the fluorescent dye Atto 488 maleimide. His-tagged Glpf and SecYEG were expressed, purified on a Ni2+-column followed (in case of SecYEG) by a size-exclusion chromatography step (Äkta Pure, column SuperDex 200 Increase100/30), and reconstituted into E.coli total lipid extract and additional 5 % DOPE-cap-biotin (Avanti Polar Lipids, Alabaster, AL, U.S.A.) as previously described25 (link), 31 (link), 40 (link). All steps including the reconstitution step were controlled by SDS-PAGE (Supplementary Fig. 1). Proteoliposomes were extruded through two stacked 100 nm polycarbonate filters (Avestin, Ottawa, Canada). Reconstitution efficiency of SecYEG and GlpF into proteoliposomes was checked by fluorescence correlation spectroscopy14 (link) (LSM 510 META/ConfoCor 3, Carl Zeiss, Jena, Germany). The reconstituted GlpF was further subjected to a functional test in a stopped flow apparatus. Its single channel water permeability was derived as previously described14 (link).
Karner A., Nimmervoll B., Plochberger B., Klotzsch E., Horner A., Knyazev D.G., Kuttner R., Winkler K., Winter L., Siligan C., Ollinger N., Pohl P, & Preiner J. (2016). Tuning membrane protein mobility by confinement into nanodomains. Nature nanotechnology, 12(3), 260-266.
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4

Fluorescence Correlation Spectroscopy for Vesicle Analysis

Cited 1 time
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FCS served to measure the average radius of vesicle ensembles and the leakage of CF from lipid vesicles after subjection to an hypoosmotic gradient. In brief, the average residence time τD of Atto633-PPE labeled vesicles and the appearance of free CF visible as a second component in the autocorrelation function G(τ) of the fluorescence temporal signals from the confocal volume, was acquired using a commercial laser scanning microscope equipped with avalanche diodes (LSM 510 META Confocor 3 with a 40x-UOPLAN water immersion objective; Carl Zeiss). The confocal volume was calibrated using the residence time of rhodamine 6G in solution and its diffusion coefficient of 426 μm2 s−1,58 (link) as previously described.59,60 (link) To this end, we applied the standard model for one- or two-component free 3D diffusion.51,61 (link)D was determined as ω2/4τD.
Wachlmayr J., Hannesschlaeger C., Speletz A., Barta T., Eckerstorfer A., Siligan C, & Horner A. (2021). Scattering versus fluorescence self-quenching: more than a question of faith for the quantification of water flux in large unilamellar vesicles?. Nanoscale Advances, 4(1), 58-76.
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5

Quantifying Membrane Channel Density

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FCS was used to determine the channel density within the GUV membrane as previously described in Ref. 33 (link). In brief, the number of YFP-labeled AQP1 was derived from the autocorrelation function ( G(τ) ) of the temporal fluorescence intensity signal, detected with a commercial laser scanning microscope (LSM 510 META ConfoCor 3 with a 40x-UOPLAN water immersion objective; Carl Zeiss, Jena, Germany) using avalanche photodiodes.
Wachlmayr J., Fläschner G., Pluhackova K., Sandtner W., Siligan C, & Horner A. (2023). Entropic barrier of water permeation through single-file channels. Communications Chemistry, 6, 135.
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