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{{STRUCTURE_4cfz|  PDB=4cfz  |  SCENE=  }}
==SAVINASE CRYSTAL STRUCTURES FOR COMBINED SINGLE CRYSTAL DIFFRACTION AND POWDER DIFFRACTION ANALYSIS==
===SAVINASE CRYSTAL STRUCTURES FOR COMBINED SINGLE CRYSTAL DIFFRACTION AND POWDER DIFFRACTION ANALYSIS===
<StructureSection load='4cfz' size='340' side='right' caption='[[4cfz]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
{{ABSTRACT_PUBMED_24699655}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4cfz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10840 Atcc 10840]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CFZ 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cfy|4cfy]], [[4cg0|4cg0]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </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=4cfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cfz RCSB], [http://www.ebi.ac.uk/pdbsum/4cfz PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SUBS_BACLE SUBS_BACLE]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A microcrystalline suspension of Bacillus lentus subtilisin (Savinase) produced during industrial large-scale production was analysed by X-ray powder diffraction (XRPD) and X-ray single-crystal diffraction (MX). XRPD established that the bulk microcrystal sample representative of the entire production suspension corresponded to space group P212121, with unit-cell parameters a = 47.65, b = 62.43, c = 75.74 A, equivalent to those for a known orthorhombic crystal form (PDB entry 1ndq). MX using synchrotron beamlines at the Diamond Light Source with beam dimensions of 20 x 20 microm was subsequently used to study the largest crystals present in the suspension, with diffraction data being collected from two single crystals ( approximately 20 x 20 x 60 microm) to resolutions of 1.40 and 1.57 A, respectively. Both structures also belonged to space group P212121, but were quite distinct from the dominant form identified by XRPD, with unit-cell parameters a = 53.04, b = 57.55, c = 71.37 A and a = 52.72, b = 57.13, c = 65.86 A, respectively, and refined to R = 10.8% and Rfree = 15.5% and to R = 14.1% and Rfree = 18.0%, respectively. They are also different from any of the forms previously reported in the PDB. A controlled crystallization experiment with a highly purified Savinase sample allowed the growth of single crystals of the form identified by XRPD; their structure was solved and refined to a resolution of 1.17 A with an R of 9.2% and an Rfree of 11.8%. Thus, there are at least three polymorphs present in the production suspension, albeit with the 1ndq-like microcrystals predominating. It is shown how the two techniques can provide invaluable and complementary information for such a production suspension and it is proposed that XRPD provides an excellent quality-control tool for such suspensions.


==Function==
Analysis of an industrial production suspension of Bacillus lentus subtilisin crystals by powder diffraction: a powerful quality-control tool.,Frankaer CG, Moroz OV, Turkenburg JP, Aspmo SI, Thymark M, Friis EP, Stahl K, Nielsen JE, Wilson KS, Harris P Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1115-23. doi:, 10.1107/S1399004714001497. Epub 2014 Mar 21. PMID:24699655<ref>PMID:24699655</ref>
[[http://www.uniprot.org/uniprot/SUBS_BACLE SUBS_BACLE]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4cfz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFZ OCA].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:024699655</ref><references group="xtra"/><references/>
*[[Subtilisin|Subtilisin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 10840]]
[[Category: Subtilisin]]
[[Category: Subtilisin]]
[[Category: Aspmo, S I.]]
[[Category: Aspmo, S I]]
[[Category: Frankaer, C G.]]
[[Category: Frankaer, C G]]
[[Category: Friis, E P.]]
[[Category: Friis, E P]]
[[Category: Harris, P.]]
[[Category: Harris, P]]
[[Category: Moroz, O V.]]
[[Category: Moroz, O V]]
[[Category: Nielsen, J E.]]
[[Category: Nielsen, J E]]
[[Category: Stahla, K.]]
[[Category: Stahla, K]]
[[Category: Thymark, M.]]
[[Category: Thymark, M]]
[[Category: Turkenburg, J P.]]
[[Category: Turkenburg, J P]]
[[Category: Wilson, K S.]]
[[Category: Wilson, K S]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Microcrystalline suspension]]
[[Category: Microcrystalline suspension]]
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