8ew0
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ew0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EW0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ew0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EW0 FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ew0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ew0 OCA], [https://pdbe.org/8ew0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ew0 RCSB], [https://www.ebi.ac.uk/pdbsum/8ew0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ew0 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ew0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ew0 OCA], [https://pdbe.org/8ew0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ew0 RCSB], [https://www.ebi.ac.uk/pdbsum/8ew0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ew0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref> | [https://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions. | ||
| - | + | ==See Also== | |
| - | + | *[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Cryo-EM structure of glutamate dehydrogenase frozen at various temperature
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Categories: Bos taurus | Large Structures | Shi H | Wu C | Zhang X
