6s2o

<table><tr><td colspan='2'>[[6s2o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cpgv Cpgv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S2O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S2O FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6s2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s2o OCA], [http://pdbe.org/6s2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s2o RCSB], [http://www.ebi.ac.uk/pdbsum/6s2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s2o ProSAT]</span></td></tr>

== 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.

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== 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>

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<div class="pdbe-citations 6s2o" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cpgv]]

[[Category: Buecker, R]]

[[Category: Hogan-Lamarre, P]]

[[Category: Mehrabi, P]]

[[Category: Schulz, E C]]

[[Category: Viral protein]]