Mini scanner

Manufactured by Bruker

The Mini-scanner is a compact and versatile imaging device designed for non-destructive evaluation and analysis. It provides high-resolution scans of small samples or areas of interest. The core function of the Mini-scanner is to capture detailed images and data for various applications, without further interpretation or extrapolation.

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Lab products found in correlation

Hit cell incubator, by Bruker (2 mentions) Ti2 inverted light microscope, by Yokogawa (1 mentions) Sr apo tirf 100x 1.49 na, by Oxford Instruments (1 mentions) Structured illumination microscope n sim, by Oxford Instruments (1 mentions) Ultra du 897 emccd camera, by Oxford Instruments (1 mentions) A1 microscope, by Nikon (1 mentions) Csu x1 spinning disk head, by Yokogawa (1 mentions)

6 protocols using mini scanner

Quantifying Microvilli Dynamics via FRAP

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ROIs of similar area were drawn over the microvilli and rootlets of W4 cells, and bleached using a 405 nm LASER steered with a Bruker mini-scanner. Cells were imaged for 30 s before photobleaching, bleached over the course of 5 s, and then imaged every 10 s for 30 min to capture signal recovery dynamics. All intensity values for each condition were normalized from 0 to 1 and plotted together to facilitate comparison. Average values for each condition were fit using two-phase association curves.

Morales E.A., Arnaiz C., Krystofiak E.S., Zanic M, & Tyska M.J. (2022). Mitotic Spindle Positioning (MISP) is an actin bundler that selectively stabilizes the rootlets of epithelial microvilli. Cell reports, 39(3), 110692.

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Quantifying Microvilli Dynamics via FRAP

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Membrane Protein Mobility Dynamics

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ROIs of similar area were drawn over the edge of HeLa cells expressing either of the three membrane binding motifs (CDHR2TM-FKBP, BTK-PH-FKBP, or FKBP-TH1) and bleached using a 405 nm LASER steered with a Bruker mini-scanner. Cells were imaged for 1 min prior to bleach and then imaged with no delay for 5 min to capture signal recovery dynamics. The first 2 min of recovery were used for analysis, and the first 50 sec of recovery are displayed on the graphs. All intensity values for each condition were normalized to the cell body intensity and background intensity as a ratio of (stimulated – background)/(cell body – background). These FRAP intensities from multiple cells were then normalized from 0 to 1 and plotted together. Average values for each condition were fit using two-phase association curves. Immobile fractions were calculated as 1 minus the plateau of the curve.

Fitz G.N., Weck M.L., Bodnya C., Perkins O.L, & Tyska M.J. (2023). Protrusion growth driven by myosin-generated force. Developmental cell, 58(1), 18-33.e6.

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Multimodal Imaging for Filopodia Analysis

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Laser scanning confocal imaging was conducted using a Nikon A1 Microscope equipped with 405, 488, 561, and 645 nm LASERs, Plan Apo 60X/1.4NA, and Plan Apo 25X/1.05 NA silicon (SIL) immersion objectives. Live-cell imaging was performed on a Nikon Ti2 inverted light microscope equipped with a Yokogawa CSU-X1 spinning disk head, equipped with 488 nm, 561 nm, and 647 nm excitation LASERs, a 405 nm photo-stimulation LASER directed by a Bruker mini-scanner to enable targeted photobleaching, a 100X Apo TIRF 100x/1.45 NA objective, and either a Hamamatsu Fusion BT or Photo-metrics Prime 95B sCMOS camera. Cells were maintained in a stage top incubator at 37°C with 5% CO2 (Tokai Hit). Super-resolution imaging was performed using a Nikon Structured Illumination Microscope (N-SIM) equipped with 405, 488, 561 and 640 nm LASERs, an SR Apo TIRF 100X/1.49 NA objective, and an Andor iXon Ultra DU-897 EMCCD camera. Images were reconstructed using Nikon Elements software. For imaging in all microscope modalities, imaging acquisition parameters were matched between samples during image acquisition. All images were denoised and deconvolved in Nikon Elements. As filopodia extremely thin structures, LUTs were optimized to facilitate visualization in figures.

Fitz G.N., Weck M.L., Bodnya C., Perkins O.L, & Tyska M.J. (2023). Protrusion growth driven by myosin-generated force. Developmental cell, 58(1), 18-33.e6.

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Quantifying Protein Dynamics via FRAP

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FRAP experiments were conducted on a Nikon swept field confocal microscope (describe above) outfitted with a Tokai Hit cell incubator and Bruker miniscanner. Actively contracting cells were maintained at 37°C in a humidified, 5% CO₂ environment. User-defined regions along cell–cell contacts (CDH2, CTNNB1, JUP, CTNNA1 and CTNNA3; Fig. 2) or Z-discs (SYNPO2 and SVIL; Fig. 7) were bleached with a 488 laser and recovery images collected every 5 s or 10 s for 10 min. FRAP data was quantified in ImageJ (NIH) and average recovery plots were measured in Excel (Microsoft). For Fig. 2, FRAP recovery plots represent data from >50 contacts from at least three separate transfections of unique cell preps. For Fig. 7, FRAP recovery plots represent data from 30 (SYNPO2) or 18 (SVIL) Z-discs from two independent transfections of unique cell preps. Curves were either fit to a double exponential formula (Fig. 2) or a single exponential formula (Fig. 7), whichever fit the recovery data the best, to determine the mobile fraction and half time of recovery in Prism (GraphPad).

Li Y., Merkel C.D., Zeng X., Heier J.A., Cantrell P.S., Sun M., Stolz D.B., Watkins S.C., Yates N.A, & Kwiatkowski A.V. (2019). The N-cadherin interactome in primary cardiomyocytes as defined using quantitative proximity proteomics. Journal of Cell Science, 132(3), jcs221606.

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Quantifying Membrane Protein Mobility

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FRAP experiments were conducted on a Nikon swept field confocal microscope (describe above) outfitted with a Tokai Hit cell incubator and Bruker miniscanner. Actively contracting cells were maintained at 37°C in a humidified, 5% CO₂ environment. User-defined regions along cell–cell contacts were bleached with a 488 laser and recovery images collected every 10 s for 15 min. FRAP data were quantified in ImageJ (National Institutes of Health [NIH]) and average recovery plots were measured in Excel (Microsoft). All recovery plots represent data from two independent transfections of unique cell preps. The data were fitted to a double-exponential curve to determine the mobile fraction and half time of recovery in Prism (GraphPad). Only recovery rates of the slow pool are reported as this was the dominant mobile pool (87–91%) for all constructs.

Merkel C.D., Li Y., Raza Q., Stolz D.B, & Kwiatkowski A.V. (2019). Vinculin anchors contractile actin to the cardiomyocyte adherens junction. Molecular Biology of the Cell, 30(21), 2639-2650.

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