| Cryo electron microscopy (28) |  |
| Structural biology (25) | |
Researchers use gold substrate to allow for electron cryomicroscopy on difficult proteins More information: Shewanella oneidensis MR-1 nanowires are outer membrane and periplasmic extensions of the extracellular electron transport components PNAS www. pnas. org/cgi/doi/10.1073
"Through a combination of high-resolution cryo-electron microscopy (CRYO EM) and a unique methodology for image analysis, a team of researchers with Berkeley Lab and the University of California (UC) Berkeley has produced an atomic view of microtubules
In this latest study, she and her group used CRYO EM in which protein samples are flash-frozen at liquid nitrogen temperatures to preserve their natural structure,
With CRYO EM and their image analysis methodology, they achieved a resolution of 3. 5 Angstroms, a record for microtubules.
"Through a combination of high-resolution cryo-electron microscopy (CRYO EM) and a unique methodology for image analysis, a team of researchers with Berkeley Lab and the University of California (UC) Berkeley has produced an atomic view of microtubules
In this latest study, she and her group used CRYO EM in which protein samples are flash-frozen at liquid nitrogen temperatures to preserve their natural structure,
With CRYO EM and their image analysis methodology, they achieved a resolution of 3. 5 Angstroms, a record for microtubules.
The team employed cryo-electron microscopy, also known as CRYO EM, to observe the particles and origami frames. This work was headed by Huilin Li, Brookhaven Lab and Stony Brook University biologist,
CRYO EM preserves samples in their near-native states and provides close to nanometer resolution. We show that CRYO EM can be applied successfully to probe the 3d structure of DNA NANOPARTICLE clusters,
Wang said. The DOE Office of Science supported the study. DOE Office of Science supports the Brookhaven National Laboratory.
or'CRYO EM'-imaging samples frozen to-180oc-to show the proteasome complex in such extraordinary detail that they could view a prototype drug bound to its active sites.
The research could help other scientists to use CRYO EM in structure-based drug design studies-in which researchers build the best possible drugs starting from a molecule which already binds to the active site of a target protein.
CRYO EM offers the opportunity to study protein complexes in conditions closer to those in the human body.
or CRYO EM, the technique had largely been written off as useless for determining the structure of very small proteins.
and other institutions have made CRYO EM a key tool in structural biology. ryo-EM has made this marked jump in the last three or four years in terms of resolution,
to use CRYO EM to visualize the structure of the body receptors that sense the spiciness of chili peppers and, in work reported last month, wasabi.
who worked with Cheng to create better cameras and software for CRYO EM. o it really a huge change in what possible. etter Camera, Better Picture Yet for a long time,
Another challenge was that earlier digital cameras used in CRYO EM detected light not electrons. So when the electron passed through the sample the signal had to be translated into light signals,
CRYO EM had previously been used to examine larger structures, like ribosomes and viruses, but this was the first membrane protein to
who does CRYO EM research at HHMI Janelia Research Campus, In virginia. Earlier this year, Cheng and Julius determined the structure of another key protein receptor,
The resolution of CRYO EM as used by Cheng and Agard is currently about 3 ångströms;
Cheng plans to use CRYO EM to examine the same molecule that Watson, Crick, and Franklin probed over 60 years ago DNA and, more specifically, chromatin, the term for DNA in complex with its associated proteins."
and I anticipate that CRYO EM will also play a significant role in this area.""Source: University of California San Francisc r
To learn more, the researchers analyzed cryo-electron microscopy (CRYO EM) structures of 2d22 in complex with two different strains of viral serotype 2--the dengue serotype with the most dynamic surface--at 6. 5
These CRYO EM structures reveal that 2d22 binds to viral envelope proteins, locking about two-thirds of them in place on the viral surface and preventing them from reorganizing into the orientations required to enter host cells.
"CRYO EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers,"by G. Fibriansah;
Now a team from Harvard Medical school, using electron cryomicroscopy (imaging frozen specimens to reduce damage from electron radiation),
Advances in electron cryomicroscopy encouraged them to try again. A team from Whelan lab, working with a group led by Stephen Harrison, Giovanni Armenise Harvard Professor of Basic Biomedical science at HMS and a Howard Hughes Medical Institute (HHMI) investigator
< Back - Next >
Overtext Web Module V3.0 Alpha
Copyright Semantic-Knowledge, 1994-2011