This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6s2o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:50, 18 November 2020) (edit) (undo)
 
Line 8: Line 8:
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GRAN_GVCPM GRAN_GVCPM]] Component of the virus occlusion bodies, which are large proteinaceous structures, that protect the virus from the outside environment for extended periods until they are ingested by insect larvae.
[[http://www.uniprot.org/uniprot/GRAN_GVCPM GRAN_GVCPM]] Component of the virus occlusion bodies, which are large proteinaceous structures, that protect the virus from the outside environment for extended periods until they are ingested by insect larvae.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from sub-micron-sized crystals. However, beam time at these facilities is scarce, and involved sample delivery techniques are required. On the other hand, rotation electron diffraction (MicroED) has shown great potential as an alternative means for protein nano-crystallography. Here, we present a method for serial electron diffraction of protein nanocrystals combining the benefits of both approaches. In a scanning transmission electron microscope, crystals randomly dispersed on a sample grid are automatically mapped, and a diffraction pattern at fixed orientation is recorded from each at a high acquisition rate. Dose fractionation ensures minimal radiation damage effects. We demonstrate the method by solving the structure of granulovirus occlusion bodies and lysozyme to resolutions of 1.55 A and 1.80 A, respectively. Our method promises to provide rapid structure determination for many classes of materials with minimal sample consumption, using readily available instrumentation.
 +
 +
Serial protein crystallography in an electron microscope.,Bucker R, Hogan-Lamarre P, Mehrabi P, Schulz EC, Bultema LA, Gevorkov Y, Brehm W, Yefanov O, Oberthur D, Kassier GH, Dwayne Miller RJ Nat Commun. 2020 Feb 21;11(1):996. doi: 10.1038/s41467-020-14793-0. PMID:32081905<ref>PMID:32081905</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6s2o" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Granulovirus occlusion bodies by serial electron diffraction

PDB ID 6s2o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools