3qyu: Difference between revisions
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[[ | ==Crystal structure of human cyclophilin D at 1.54 A resolution at room temperature== | ||
<StructureSection load='3qyu' size='340' side='right' caption='[[3qyu]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qyu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QYU FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qyw|3qyw]], [[3qyz|3qyz]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIF, CYP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3qyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qyu RCSB], [http://www.ebi.ac.uk/pdbsum/3qyu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-ray crystallography is now a recognized technique for ligand screening, especially for fragment-based drug design. However, protein crystal handling is still tedious and limits further automation. An alternative method for the solution of crystal structures of proteins in complex with small ligands is proposed. Crystallization drops are directly exposed to an X-ray beam after cocrystallization or soaking with the desired ligands. The use of dedicated plates in connection with an optimal parametrization of the G-rob robot allows efficient data collection. Three proteins currently under study in our laboratory for ligand screening by X-ray crystallography were used as validation test cases. The protein crystals belonged to different space groups, including a challenging monoclinic case. The resulting diffraction data can lead to clear ligand recognition, including indication of alternating conformations. These results demonstrate a possible method for automation of ligand screening by X-ray crystallography. | |||
In-plate protein crystallization, in situ ligand soaking and X-ray diffraction.,le Maire A, Gelin M, Pochet S, Hoh F, Pirocchi M, Guichou JF, Ferrer JL, Labesse G Acta Crystallogr D Biol Crystallogr. 2011 Sep;67(Pt 9):747-55. doi:, 10.1107/S0907444911023249. Epub 2011 Aug 9. PMID:21904027<ref>PMID:21904027</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Cyclophilin|Cyclophilin]] | *[[Cyclophilin|Cyclophilin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Colliandre, L | [[Category: Colliandre, L]] | ||
[[Category: Gelin, M | [[Category: Gelin, M]] | ||
[[Category: Guichou, J F | [[Category: Guichou, J F]] | ||
[[Category: Labesse, G | [[Category: Labesse, G]] | ||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Mitochondria]] | [[Category: Mitochondria]] | ||
[[Category: Prolyl cis/trans isomerase]] | [[Category: Prolyl cis/trans isomerase]] | ||