Crystallization and a preliminary X-ray crystallographic study of alpha-amylase from Bacillus licheniformis.
alpha-Amylase from Bacillus licheniformis has been crystallized by the hanging-drop vapor diffusion method in the presence of calcium ions using ammonium sulfate as precipitant. The crystals are tetragonal, belonging to the space group P4(1)2(1)2 (or P4(3)2(1)2), with unit cell dimensions of a = 119.9 and c = 85.4 A. The asymmetric unit contains one molecule of alpha-amylase, with a crystal volume per protein mass (VM) of 2.78 A3/Da. The crystals diffract to better than 2.0 A Bragg spacing when exposed to synchrotron X-rays and they are reasonably stable in the X-ray beam. Thus the crystals are suitable for structure determination at high resolution by X-ray methods.
Lee
S Y
SY
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.
Kim
S
S
Sweet
R M
RM
Suh
S W
SW
D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D014961:X-Ray Diffraction; D000516:alpha-Amylases / Q000737:chemistry / Q000302:isolation & purification*
D000516:alpha-Amylases