5a1a: Difference between revisions
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==2.2 A resolution cryo-EM structure of beta- | ==2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor== | ||
<StructureSection load='5a1a' size='340' side='right' caption='[[5a1a]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5a1a' size='340' side='right' caption='[[5a1a]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a1a RCSB], [http://www.ebi.ac.uk/pdbsum/5a1a PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a1a RCSB], [http://www.ebi.ac.uk/pdbsum/5a1a PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cryo-electron microscopy (cryo-EM) is rapidly emerging as a powerful tool for protein structure determination at high resolution. Here, we report the structure of a complex between Escherichia coli beta-galactosidase and the cell-permeant inhibitor phenylethyl beta-d-thiogalactopyranoside (PETG), determined by cryo-EM at a resolution of ~2.2 A. Besides the PETG ligand, we identified densities in the map for ~800 water molecules and for magnesium and sodium ions. While it is likely that continued advances in detector technology may further enhance resolution, our findings demonstrate that preparation of specimens of adequate quality and intrinsic protein flexibility, rather than imaging or image processing technologies, now represent the major bottlenecks to achieving resolutions close to 2 A using single particle cryo-EM. | |||
2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor.,Bartesaghi A, Merk A, Banerjee S, Matthies D, Wu X, Milne JL, Subramaniam S Science. 2015 May 7. pii: aab1576. PMID:25953817<ref>PMID:25953817</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:30, 20 May 2015
2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor
Structural highlights
Publication Abstract from PubMedCryo-electron microscopy (cryo-EM) is rapidly emerging as a powerful tool for protein structure determination at high resolution. Here, we report the structure of a complex between Escherichia coli beta-galactosidase and the cell-permeant inhibitor phenylethyl beta-d-thiogalactopyranoside (PETG), determined by cryo-EM at a resolution of ~2.2 A. Besides the PETG ligand, we identified densities in the map for ~800 water molecules and for magnesium and sodium ions. While it is likely that continued advances in detector technology may further enhance resolution, our findings demonstrate that preparation of specimens of adequate quality and intrinsic protein flexibility, rather than imaging or image processing technologies, now represent the major bottlenecks to achieving resolutions close to 2 A using single particle cryo-EM. 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor.,Bartesaghi A, Merk A, Banerjee S, Matthies D, Wu X, Milne JL, Subramaniam S Science. 2015 May 7. pii: aab1576. PMID:25953817[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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