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| | ==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]] 1.57Å' scene=''> | + | <StructureSection load='4cfz' size='340' side='right'caption='[[4cfz]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[4cfz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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'>[https://proteopedia.org/fgij/fg.htm?mol=4cfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfz OCA], [https://pdbe.org/4cfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cfz RCSB], [https://www.ebi.ac.uk/pdbsum/4cfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cfz ProSAT]</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://pdbe.org/4cfz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cfz RCSB], [http://www.ebi.ac.uk/pdbsum/4cfz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cfz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 10840]] | + | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]] | + | [[Category: Lederbergia lenta]] |
| - | [[Category: Aspmo, S I]] | + | [[Category: Aspmo SI]] |
| - | [[Category: Frankaer, C G]] | + | [[Category: Frankaer CG]] |
| - | [[Category: Friis, E P]] | + | [[Category: Friis EP]] |
| - | [[Category: Harris, P]] | + | [[Category: Harris P]] |
| - | [[Category: Moroz, O V]] | + | [[Category: Moroz OV]] |
| - | [[Category: Nielsen, J E]] | + | [[Category: Nielsen JE]] |
| - | [[Category: Stahla, K]] | + | [[Category: Stahla K]] |
| - | [[Category: Thymark, M]] | + | [[Category: Thymark M]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Wilson, K S]] | + | [[Category: Wilson KS]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Microcrystalline suspension]]
| + | |
| - | [[Category: Powder diffraction]]
| + | |
| - | [[Category: Quality control]]
| + | |
| - | [[Category: Single crystal analysis]]
| + | |
| Structural highlights
Function
SUBS_LEDLE Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frankaer CG, Moroz OV, Turkenburg JP, Aspmo SI, Thymark M, Friis EP, Stahl K, Nielsen JE, Wilson KS, Harris P. Analysis of an industrial production suspension of Bacillus lentus subtilisin crystals by powder diffraction: a powerful quality-control tool. Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1115-23. doi:, 10.1107/S1399004714001497. Epub 2014 Mar 21. PMID:24699655 doi:http://dx.doi.org/10.1107/S1399004714001497
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