Preliminary X-ray crystallographic analysis of a novel maltogenic amylase from Bacillus stearothermophilus ET1

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A novel maltogenic amylase from Bacillus stearothermophilus ET1, which has a dual activity of alpha-1,4- and alpha-1,6-glycosidic bond cleavages and alpha-1,6-glycosidic bond formation, was crystallized by using the hanging-drop vapor-diffusion method. The best crystals were obtained by employing a high concentration of protein (56 mg ml(-1)) and a precipitant containing 22% glycerol, 1.6 M ammonium sulfate in 0.1 M Tris-HCl (pH 8.5). Native diffraction data to 2.66 Angstrom resolution have been obtained from crystals flash-frozen at 110 K. The crystals belong to the space group P2(1)2(1)2(1) pith unit-cell dimensions of a = 77.62, b = 121.23, c = 244.29 Angstrom, and contain three or four protomers per asymmetric unit. Structure determination by multiple isomorphous replacement is in progress.
Publisher
MUNKSGAARD INT PUBL LTD
Issue Date
1998-05
Language
English
Article Type
Article
Keywords

PANCREATIC ALPHA-AMYLASE; AWAMORI VAR X100; 2.2-ANGSTROM RESOLUTION; BETA-AMYLASE; MOLECULAR REPLACEMENT; ANGSTROM RESOLUTION; REFINED STRUCTURE; CRYSTAL-STRUCTURE; ACTIVE-SITE; GLUCOAMYLASE

Citation

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.54, pp.416 - 418

ISSN
0907-4449
DOI
10.1107/S0907444997011736
URI
http://hdl.handle.net/10203/74521
Appears in Collection
BS-Journal Papers(저널논문)
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