2a6u

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(New page: 200px<br /><applet load="2a6u" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a6u, resolution 3.28&Aring;" /> '''pH evolution of tetr...)
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[[Image:2a6u.gif|left|200px]]<br /><applet load="2a6u" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2a6u, resolution 3.28&Aring;" />
 
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'''pH evolution of tetragonal HEWL at 4 degrees Celcius.'''<br />
 
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==Overview==
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==pH evolution of tetragonal HEWL at 4 degrees Celcius.==
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44 samples of tetragonal hen egg-white lysozyme (HEWL) were obtained as a, series of polycrystalline precipitates at 277 K and room temperature in, the pH range between 6.56 and 3.33. The precipitates were investigated by, the collection of high-resolution powder X-ray diffraction data at 295 K, which reveal the tetragonal or orthorhombic forms of lysozyme depending on, the temperature and pH of crystallization. The use of a new robotic sample, changer greatly facilitated these measurements. LeBail analyses of the, powder patterns display a characteristic behaviour for the pH dependence, of the tetragonal unit-cell parameters of HEWL crystallized at both, temperatures. More detailed analysis shows that molecular replacement can, give a suitable starting point for structural refinements, illustrating, that powder data can be sufficient for this approach. Pawley or Rietveld, refinements that fit a single model to four data sets simultaneously from, four samples crystallized at pH values across the range studied benefit, from improved powder data quality via the anisotropic changes in the unit, cell. The Rietveld analysis gave an average structural model with, excellent goodness of fit and stereochemistry.
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<StructureSection load='2a6u' size='340' side='right'caption='[[2a6u]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2a6u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6U FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray powder diffraction</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6u OCA], [https://pdbe.org/2a6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6u RCSB], [https://www.ebi.ac.uk/pdbsum/2a6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/2a6u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2a6u ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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44 samples of tetragonal hen egg-white lysozyme (HEWL) were obtained as a series of polycrystalline precipitates at 277 K and room temperature in the pH range between 6.56 and 3.33. The precipitates were investigated by the collection of high-resolution powder X-ray diffraction data at 295 K, which reveal the tetragonal or orthorhombic forms of lysozyme depending on the temperature and pH of crystallization. The use of a new robotic sample changer greatly facilitated these measurements. LeBail analyses of the powder patterns display a characteristic behaviour for the pH dependence of the tetragonal unit-cell parameters of HEWL crystallized at both temperatures. More detailed analysis shows that molecular replacement can give a suitable starting point for structural refinements, illustrating that powder data can be sufficient for this approach. Pawley or Rietveld refinements that fit a single model to four data sets simultaneously from four samples crystallized at pH values across the range studied benefit from improved powder data quality via the anisotropic changes in the unit cell. The Rietveld analysis gave an average structural model with excellent goodness of fit and stereochemistry.
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==About this Structure==
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High-throughput phase-diagram mapping via powder diffraction: a case study of HEWL versus pH.,Basso S, Fitch AN, Fox GC, Margiolaki I, Wright JP Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1612-25. Epub 2005, Nov 19. PMID:16301795<ref>PMID:16301795</ref>
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2A6U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A6U OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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High-throughput phase-diagram mapping via powder diffraction: a case study of HEWL versus pH., Basso S, Fitch AN, Fox GC, Margiolaki I, Wright JP, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1612-25. Epub 2005, Nov 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16301795 16301795]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 2a6u" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Margiolaki, I.]]
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[[Category: lysozyme]]
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[[Category: powder diffraction]]
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[[Category: rietveld refinement]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:56:59 2007''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Margiolaki I]]

Current revision

pH evolution of tetragonal HEWL at 4 degrees Celcius.

PDB ID 2a6u

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