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

Breaking the 3 Å barrier

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

Artifact-free diffraction rings

Artifact-free diffraction rings
The Rio camera offers diffraction rings free from artifacts associated with CCD or other CMOS artifacts. Due to low noise floor, diffraction rings not usually visible in Au sample can be seen without artifacts from the central spot.

Choose the right FOV for your application

Choose the right FOV for your application
The Rio camera offers three cameras with both side and bottom mount. This allows you to pick the exact FOV that you need for your experiments.

Capture high-resolution detail with the largest FOV

Capture high-resolution detail with the largest FOV
There is no need to go to high magnification to resolve fine features. The Rio camera offers low noise with a high dynamic range.

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.

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