Negative stain EM was used to assess sample quality of PSI monomer preparations. An aliquot of 3.5 μl ~100x diluted protein solution was applied to glow-discharged (10 s at 5 mA) continuous carbon film-coated copper grids (Nisshin EM) and stained using a 2% (w/w) uranyl acetate solution. After brief blotting (Whatman #1) the grid was air-dried and examined on an H-7650 HITACHI electron microscope at 80 kV, equipped with a 1 × 1 k Tietz FastScan-F114 CCD camera (TVIPS, Gauting, Germany).
Fastscan f114 ccd camera
Manufactured by TVIPS
Sourced in Germany
The FastScan-F114 CCD camera is a high-performance imaging device designed for scientific and industrial applications. It features a 14-megapixel CCD sensor with a pixel size of 6.5 μm. The camera offers a fast readout speed of up to 30 frames per second and a wide dynamic range. The FastScan-F114 is capable of capturing detailed, high-quality images and is intended for use in various imaging and analysis tasks.
Automatically generated - may contain errors
Lab products found in correlation
3 protocols using fastscan f114 ccd camera
1
Negative Stain Electron Microscopy for Protein Quality
2
Visualization and Analysis of PomA Flagellar Motor
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Elution fractions of WT and PomA-F66S mutations were diluted in SEC buffer.
Final concentration of the samples in the WT and F66S mutation were 3.4 and 5.3 ng/mL, respectively. A 5 μL solution was applied to a glow-discharged continuous carbon grid. The excess solution was removed using filter paper, and the sample was subsequently stained on the carbon grid with 2% ammonium molybdate. Electron microscopy images were recorded with an H-7650 transmission electron microscope (Hitachi) operated at 80 kV and equipped with a FastScan-F114 CCD camera (TVIPS, Gauting, Germany) at a nominal magnification of 80,000 ×. flagellar motor. J Bacteriol 190: 3565-3571. with mutations were grown to the mid-log phase. The proteins of the cells were then separated using sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) and detected via western blotting using the anti-PomA antibody. arabinose was added at a final concentration of 0.02% (w/v), 2 h later, to induce expression (arrow). A 660 was measured every 1 h after induction. preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
Final concentration of the samples in the WT and F66S mutation were 3.4 and 5.3 ng/mL, respectively. A 5 μL solution was applied to a glow-discharged continuous carbon grid. The excess solution was removed using filter paper, and the sample was subsequently stained on the carbon grid with 2% ammonium molybdate. Electron microscopy images were recorded with an H-7650 transmission electron microscope (Hitachi) operated at 80 kV and equipped with a FastScan-F114 CCD camera (TVIPS, Gauting, Germany) at a nominal magnification of 80,000 ×. flagellar motor. J Bacteriol 190: 3565-3571. with mutations were grown to the mid-log phase. The proteins of the cells were then separated using sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) and detected via western blotting using the anti-PomA antibody. arabinose was added at a final concentration of 0.02% (w/v), 2 h later, to induce expression (arrow). A 660 was measured every 1 h after induction. preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
3
Visualization and Analysis of PomA Flagellar Motor
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Elution fractions of WT and PomA-F66S mutations were diluted in SEC buffer.
Final concentration of the samples in the WT and F66S mutation were 3.4 and 5.3 ng/mL, respectively. A 5 μL solution was applied to a glow-discharged continuous carbon grid. The excess solution was removed using filter paper, and the sample was subsequently stained on the carbon grid with 2% ammonium molybdate. Electron microscopy images were recorded with an H-7650 transmission electron microscope (Hitachi) operated at 80 kV and equipped with a FastScan-F114 CCD camera (TVIPS, Gauting, Germany) at a nominal magnification of 80,000 ×. flagellar motor. J Bacteriol 190: 3565-3571. with mutations were grown to the mid-log phase. The proteins of the cells were then separated using sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) and detected via western blotting using the anti-PomA antibody. arabinose was added at a final concentration of 0.02% (w/v), 2 h later, to induce expression (arrow). A 660 was measured every 1 h after induction. preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
Final concentration of the samples in the WT and F66S mutation were 3.4 and 5.3 ng/mL, respectively. A 5 μL solution was applied to a glow-discharged continuous carbon grid. The excess solution was removed using filter paper, and the sample was subsequently stained on the carbon grid with 2% ammonium molybdate. Electron microscopy images were recorded with an H-7650 transmission electron microscope (Hitachi) operated at 80 kV and equipped with a FastScan-F114 CCD camera (TVIPS, Gauting, Germany) at a nominal magnification of 80,000 ×. flagellar motor. J Bacteriol 190: 3565-3571. with mutations were grown to the mid-log phase. The proteins of the cells were then separated using sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) and detected via western blotting using the anti-PomA antibody. arabinose was added at a final concentration of 0.02% (w/v), 2 h later, to induce expression (arrow). A 660 was measured every 1 h after induction. preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
About PubCompare
Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.
We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.
However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.
Ready to get started?
Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required
Revolutionizing how scientists
search and build protocols!