Crystallization and preliminary x-ray analysis of beta-amylase from Bacillus polymyxa.
作者信息
Yamane T, Tasaki H, Matsumoto F, Suzuki A, Uozumi N, Ashida T
机构信息
Department of Biotechnology and Biomaterial Chemistry, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya 464-8603, Japan.
出版信息
Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):898-900. doi: 10.1107/s0907444998017570.
A truncated beta-amylase (E.C. 3.2.1.2) from Bacillus polymyxa has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals belong to the orthorhombic space group P212121 with cell dimensions a = 64.6, b = 141.9, c = 155.1 A and diffract to 2.5 A resolution. The asymmetric unit containing three protein molecules was derived from an electron-density map calculated at 4 A resolution using MIR phases. This gives a Vm value of 2.36 A3 Da-1.
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