2w6h
From Proteopedia
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- | [[ | + | ==LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 4A.== |
+ | <StructureSection load='2w6h' size='340' side='right' caption='[[2w6h]], [[Resolution|resolution]] 5.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2w6h]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W6H FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jiz|2jiz]], [[2v7q|2v7q]], [[1nbm|1nbm]], [[1bmf|1bmf]], [[2jj1|2jj1]], [[1e1q|1e1q]], [[1w0j|1w0j]], [[1cow|1cow]], [[1h8h|1h8h]], [[1e1r|1e1r]], [[1ohh|1ohh]], [[1qo1|1qo1]], [[2jdi|2jdi]], [[1h8e|1h8e]], [[1efr|1efr]], [[2jj2|2jj2]], [[1e79|1e79]], [[2ck3|2ck3]], [[1w0k|1w0k]], [[2w6e|2w6e]], [[2w6f|2w6f]], [[2w6g|2w6g]], [[2w6i|2w6i]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6h RCSB], [http://www.ebi.ac.uk/pdbsum/2w6h PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/2w6h_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Dehydration of protein crystals is rarely used, despite being a post-crystallization method that is useful for the improvement of crystal diffraction properties, as it is difficult to reproduce and monitor. A novel device for hydration control of macromolecular crystals in a standard data-collection environment has been developed. The device delivers an air stream of precise relative humidity that can be used to alter the amount of water in macromolecular crystals. The device can be rapidly installed and is fully compatible with most standard synchrotron X-ray beamlines. Samples are mounted in cryoloops and the progress of dehydration can be monitored both optically and by the acquisition of diffraction images. Once the optimal hydration level has been obtained, cryocooling is easy to achieve by hand or by using a sample changer. The device has been thoroughly tested on several ESRF beamlines and is available to users. | ||
- | + | Improving diffraction by humidity control: a novel device compatible with X-ray beamlines.,Sanchez-Weatherby J, Bowler MW, Huet J, Gobbo A, Felisaz F, Lavault B, Moya R, Kadlec J, Ravelli RB, Cipriani F Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1237-46. Epub 2009, Nov 17. PMID:19966409<ref>PMID:19966409</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
- | *[[ | + | *[[ATPase|ATPase]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Bowler, M W.]] | [[Category: Bowler, M W.]] |
Revision as of 10:18, 29 September 2014
LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 4A.
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Categories: Bos taurus | Bowler, M W. | Cipriani, F. | Felisaz, F. | Gobbo, A. | Huet, J. | Ravelli, R B.G. | Sanchez-Weatherby, J. | Atp phosphorylase | Atp synthase | Atp synthesis | Atp-binding | F1fo atp synthase | Hydrogen ion transport | Hydrolase | Ion transport | Mitochondrion | Nucleotide-binding | P-loop | Pyrrolidone carboxylic acid | Transit peptide | Ubl conjugation