1scd
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(New page: 200px<br /><applet load="1scd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1scd, resolution 2.3Å" /> '''X-RAY CRYSTAL STRUCTU...)
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Revision as of 00:09, 21 November 2007
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X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE
Overview
The crystal structure of subtilisin Carlsberg lightly cross-linked with, glutaraldehyde was solved in aqueous solution by X-ray crystallography at, 2.3 A resolution. It was found to be virtually identical to the recently, determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the, cross-linked enzyme in anhydrous acetonitrile. The latter structure was, found to be significantly more rigid than in water, as reflected by their, average B factors. The numbers of subtilisin-bound water molecules in the, two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are, distinct.
About this Structure
1SCD is a Single protein structure of sequence from Bacillus licheniformis with CA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile., Fitzpatrick PA, Ringe D, Klibanov AM, Biochem Biophys Res Commun. 1994 Jan 28;198(2):675-81. PMID:8297378
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