Scientists reach 2.2 Å using cryo-electron microscopy

Scientists reach 2.2 Å using cryo-electron microscopy
Bartesaghi et al., Science 348 (6239): 1147-1151

2.2 Å resolution single-particle reconstruction of β-galactosidase enabled by GIF Quantum LS imaging filter with K2 Summit camera.

Au nanocrystal reorientation

Au nanocrystal reorientation
Video courtesy JEOL Japan and Gatan, Inc., US

A single full field of view image (left) shows the high sensitivity and high signal-to-noise in a 40 ms frame. The right image is a single frame from a video that showcases step motion on the surface of a Au nanocrystal under the electron beam. 

Sample: gold (Au) nanoparticles; beam energy: 300 kV; original image size: 4k x 4k; frame rate: 25 fps

First 3D single-particle reconstruction of 20S Proteasome at 2.8 Å resolution

First 3D single-particle reconstruction of 20S Proteasome at 2.8 Å resolution
Image courtesy of Melody Campbell and the National Resource for Automated Molecular Microscopy, US.

The above series of images show a 3D reconstruction of the 20S proteasome at 2.8 Å resolution. On the right, the oxygen atom (red) found in a single water molecule is separated from the surrounding structure by 3.1 and 3.4 Å, respectively. Studying this molecule at high resolution demonstrates that scientists can identify water molecules and hydrogen bonding in structures solved by cryo-EM using the K2 Summit camera. eLife 2015;4:e06380

First ~700 kDa protein structure with D7 symmetry identified at 3.3 Å resolution using cryo-EM

K2 camera helps identify first ~700 kDa protein structure with D7 symmetry at 3.3 Å resolution using cryo-EM
Li, X.; Mooney, P.; Zheng, S.; Booth, C. R.; Braunfeld, M. B.; Gubbens, S.; Agard, D. A.; Cheng, Y.

Using the K2 Summit® camera, single-particle cryo-EM was able to match the x-ray crystallography result. (d) Portion of the cryo-EM density map showing clear side-chain densities. The docked atomic structure was refined to fit the density map by a molecular dynamic flexible fitting procedure.

First 3.4 Å TRPV1 structure solved by cryo-EM

First 3.4 Å TRPV1 structure solved by cryo-EM
Liao, M.; Cao, E.; Julius, D.; Cheng, Y.

K2 Summit camera was used to determine the structure of a mammalian TRP channel, TRPV1, at 3.4 Å resolution, breaking the side-chain resolution barrier for membrane proteins without crystallization. Nature 504, 107–112, 2013

High resolution image of a zeolite sample containing small metal Pt particles

High resolution image of a zeolite sample containing small metal Pt particles

Chevron zeolite SSZ-57

Methods

Image was captured with OneView® camera
TEM magnification: 255kx
Electron energy: 200 keV
Exposure time: 2 s
Drift correction: On

High-resolution image of C. elegans stomach sample

High-resolution image of C. elegans stomach sample

Captured with the Rio 16 camera; 200 kV; TEM indicated magnification: 6.3kx; image size: 4k x 4k; exposure time: 1 s.

Live drift correction and full resolution image display on the Rio camera

Live drift correction and full resolution image display on the Rio camera

OnPoint detector minimizes charging and beam damage

OnPoint detector minimizes charging and beam damage
Image courtesy of T. Deerinck NCMIR/UCSD.

Image shows that the OnPoint BSE detector can resolve features at 1.1 kV (right) that were previously distorted (e.g., black spots) by charging or beam damage at 2.2 kV (left). Sample: Mouse cerebellum. 

OnPoint increases 3View imaging speed four-fold

OnPoint increases 3View imaging speed four-fold

Compares image quality from the 1st generation 3View® detector (top) to the OnPoint™ detector (bottom) at various dwell times. Results show the OnPoint detector delivers equal or better resolution images using shorter dwell times (0.5 vs. 2.0 µs). Sample: Brain, 3 kV, 15 kx, 0.5 µs dwell time.

Pages