3kgg
From Proteopedia
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| - | + | ==X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): Perdeuteration of proteins for neutron diffraction== | |
| - | + | <StructureSection load='3kgg' size='340' side='right' caption='[[3kgg]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3kgg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Loligo_vulgaris Loligo vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KGG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diisopropyl-fluorophosphatase Diisopropyl-fluorophosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.2 3.1.8.2] </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=3kgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kgg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kgg RCSB], [http://www.ebi.ac.uk/pdbsum/3kgg 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/kg/3kgg_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 == | ||
| + | The signal-to-noise ratio is one of the limiting factors in neutron macromolecular crystallography. Protein perdeuteration, which replaces all H atoms with deuterium, is a method of improving the signal-to-noise ratio of neutron crystallography experiments by reducing the incoherent scattering of the hydrogen isotope. Detailed analyses of perdeuterated and hydrogenated structures are necessary in order to evaluate the utility of perdeuterated crystals for neutron diffraction studies. The room-temperature X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase) is reported at 2.1 A resolution. Comparison with an independently refined hydrogenated room-temperature structure of DFPase revealed no major systematic differences, although the crystals of perdeuterated DFPase did not diffract neutrons. The lack of diffraction is examined with respect to data-collection and crystallographic parameters. The diffraction characteristics of successful neutron structure determinations are presented as a guideline for future neutron diffraction studies of macromolecules. X-ray diffraction to beyond 2.0 A resolution appears to be a strong predictor of successful neutron structures. | ||
| - | + | X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction.,Blum MM, Tomanicek SJ, John H, Hanson BL, Ruterjans H, Schoenborn BP, Langan P, Chen JC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt, 4):379-85. Epub 2010 Mar 26. PMID:20383004<ref>PMID:20383004</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Diisopropyl-fluorophosphatase]] | [[Category: Diisopropyl-fluorophosphatase]] | ||
[[Category: Loligo vulgaris]] | [[Category: Loligo vulgaris]] | ||
| - | [[Category: Blum, M M | + | [[Category: Blum, M M]] |
| - | [[Category: Chen, J C.H | + | [[Category: Chen, J C.H]] |
| - | [[Category: Hanson, B L | + | [[Category: Hanson, B L]] |
| - | [[Category: John, H | + | [[Category: John, H]] |
| - | [[Category: Langan, P | + | [[Category: Langan, P]] |
| - | [[Category: Schoenborn, B P | + | [[Category: Schoenborn, B P]] |
| - | [[Category: Tomanicek, S J | + | [[Category: Tomanicek, S J]] |
| - | [[Category: Terjans, H R | + | [[Category: Terjans, H R]] |
[[Category: Beta propeller]] | [[Category: Beta propeller]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Phosphotriesterase]] | [[Category: Phosphotriesterase]] | ||
Revision as of 15:40, 18 December 2014
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): Perdeuteration of proteins for neutron diffraction
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