ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
A novel maltogenic amylase from Bacillus stearothermophilus ET1, which has a dual activity of α-1,4- and α-1,6-glycosidic bond cleavages and α-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 Å resolution have been obtained from crystals flash-frozen at 110 K. The crystals belong to the space group P212121 with unit-cell dimensions of a = 77.62, b = 121.23, c = 244.29 Å, and contain three or four protomers per asymmetric unit. Structure determination by multiple isomorphous replacement is in progress.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444997011736
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