Document Detail

Crystallization and preliminary X-ray analysis of beta-glucan exohydrolase isoenzyme ExoI from barley (Hordeum vulgare).
MedLine Citation:
PMID:  9761876     Owner:  NLM     Status:  MEDLINE    
Crystals of a beta-glucan exohydrolase purified from extracts of young barley seedlings have been obtained by vapour diffusion in the presence of ammonium sulfate and polyethylene glycol. The enzyme exhibits broad substrate specificity against (1,3)-, (1,3;1,4)- and (1,3;1,6)-beta-glucans, and related oligosaccharides. Crystal dimensions of up to 0.8 x 0.4 x 0.6 mm have been observed. The crystals belong to the tetragonal space group P41212 or P43212. Cell parameters are a = b = 102.1 and c = 184.5 A, and there appear to be eight molecules in the asymmetric unit. The crystals diffract to at least 2.2 A resolution using X-rays from a rotating-anode generator.
M Hrmova; J N Varghese; P B Høj; G B Fincher
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta crystallographica. Section D, Biological crystallography     Volume:  54     ISSN:  0907-4449     ISO Abbreviation:  Acta Crystallogr. D Biol. Crystallogr.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-12-14     Completed Date:  1998-12-14     Revised Date:  2007-07-24    
Medline Journal Info:
Nlm Unique ID:  9305878     Medline TA:  Acta Crystallogr D Biol Crystallogr     Country:  DENMARK    
Other Details:
Languages:  eng     Pagination:  687-9     Citation Subset:  IM    
Department of Plant Science, University of Adelaide, Waite Campus, SA 5064, Australia.
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MeSH Terms
Crystallography, X-Ray
Glucan 1,3-beta-Glucosidase
Hordeum / enzymology*
Isoenzymes / chemistry*,  isolation & purification
Plant Proteins / chemistry*,  isolation & purification
Protein Conformation
beta-Glucosidase / chemistry*,  isolation & purification
Reg. No./Substance:
0/Isoenzymes; 0/Plant Proteins; EC; EC 1,3-beta-Glucosidase

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