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|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)|
|Citation:||Acta Crystallographica Section D, Biological Crystallography, 1998; D54(4):687-689|
|Publisher:||MUNKSGAARD INT PUBL LTD|
|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|
|Appears in Collections:||Agriculture, Food and Wine publications|
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