Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/13308
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Type: Journal article
Title: Crystallization and preliminary X-ray analysis of β-glucan exohydrolase isoenzyme Exol from barley (Hordeum vulgare)
Other Titles: Crystallization and preliminary X-ray analysis of beta-glucan exohydrolase isoenzyme Exol from barley (Hordeum vulgare)
Author: Hrmova, M.
Varghese, J.
Hoj, P.
Fincher, G.
Citation: Acta Crystallographica Section D, Biological Crystallography, 1998; D54(4):687-689
Publisher: MUNKSGAARD INT PUBL LTD
Issue Date: 1998
ISSN: 0907-4449
1399-0047
Statement of
Responsibility: 
Maria Hrmova, Joseph N. Varghese, Peter B. Høj and Geoffrey B. Fincher
Abstract: Crystals of a β-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)-β-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 Å, and there appear to be eight molecules in the asymmetric unit. The crystals diffract to at least 2.2 Å resolution using X-rays from a rotating-anode generator.
Keywords: Hordeum; beta-Glucosidase; Glucan 1,3-beta-Glucosidase; Isoenzymes; Plant Proteins; Crystallization; Crystallography, X-Ray; Protein Conformation
Rights: © 1998 International Union of Crystallography
RMID: 0030003743
DOI: 10.1107/S0907444997018866
Appears in Collections:Agriculture, Food and Wine publications

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