| Literature DB >> 14993697 |
Masatake Akita1, Masahiro Mizuno, Takashi Tonozuka, Yoshiyuki Sakano, Hirokazu Matsui, Yuko Hidaka, Yuji Hatada, Susumu Ito, Koki Horikoshi.
Abstract
A recombinant isomaltodextranase (1,6-alpha-D-glucan isomaltohydrolase; EC 3.2.1.94) from an Arthrobacter sp. that hydrolyzes dextrans to generate isomaltose was purified and crystallized using the sitting-drop vapour-diffusion method at 293 K. X-ray diffraction data were collected to 1.8 A. The crystals belong to space group C2, with unit-cell parameters a = 199.1, b = 62.7, c = 57.4, beta = 101.4 degrees. Analysis of the Patterson self-rotation function suggests that the crystal contains one protein molecule in the asymmetric unit.Entities:
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Year: 2004 PMID: 14993697 DOI: 10.1107/S090744490400006X
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449