1bwi

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(New page: 200px<br /><applet load="1bwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwi, resolution 1.80&Aring;" /> '''THE 1.8 A STRUCTURE ...)
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[[Image:1bwi.gif|left|200px]]<br /><applet load="1bwi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bwi, resolution 1.80&Aring;" />
 
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'''THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME'''<br />
 
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==Overview==
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==THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME==
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A number of methods can be used to improve the stability of the protein, crystal-growth environment, including growth in microgravity without an, air-liquid phase boundary, growth in gels and growth under oil, ('microbatch'). In this study, X-ray data has been collected from and, structures refined for crystals of hen egg-white lysozyme (HEWL) grown, using four different methods, liquid-liquid dialysis on Earth and in, microgravity using the European Space Agency's (ESA) Advanced Protein, Crystallization Facility (APCF) on board the NASA Space Shuttle Life and, Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose, gel using a tube liquid-gel diffusion method and crystallization in, microbatch under oil. A comparison of the overall quality of the X-ray, data, the protein structures and especially the bound-water structures has, been carried out at 1.8 A. The lysozyme protein structures corresponding, to these four different crystallization methods remain similar. A small, improvement in the bound-solvent structure is seen in lysozyme crystals, grown in microgravity by liquid-liquid dialysis, which has a more stable, fluid physics state in microgravity, and is consistent with a better, formed protein crystal in microgravity.
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<StructureSection load='1bwi' size='340' side='right'caption='[[1bwi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bwi]] 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=1BWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWI 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 diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1bwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwi OCA], [https://pdbe.org/1bwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwi RCSB], [https://www.ebi.ac.uk/pdbsum/1bwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwi 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/bw/1bwi_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=1bwi 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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A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air-liquid phase boundary, growth in gels and growth under oil ('microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid-liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid-gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 A. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid-liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.
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==About this Structure==
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Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution.,Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):745-52. PMID:10089304<ref>PMID:10089304</ref>
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1BWI 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=1BWI 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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Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution., Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):745-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10089304 10089304]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 1bwi" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Bi, R.C.]]
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[[Category: Boggon, T.J.]]
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[[Category: Chayen, N.E.]]
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[[Category: Dong, J.]]
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[[Category: Raftery, J.]]
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[[Category: 1]]
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[[Category: 4-beta-n-acetylmuramidase c]]
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[[Category: lysozyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:58:29 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: Bi RC]]
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[[Category: Boggon TJ]]
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[[Category: Chayen NE]]
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[[Category: Dong J]]
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[[Category: Raftery J]]

Current revision

THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME

PDB ID 1bwi

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