Literature DB >> 14993697

Crystallization and preliminary X-ray study of isomaltodextranase from Arthrobacter globiformis.

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.

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Year:  2004        PMID: 14993697     DOI: 10.1107/S090744490400006X

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Crystal Structure and Mutational Analysis of Isomalto-dextranase, a Member of Glycoside Hydrolase Family 27.

Authors:  Yuka Okazawa; Takatsugu Miyazaki; Gaku Yokoi; Yuichi Ishizaki; Atsushi Nishikawa; Takashi Tonozuka
Journal:  J Biol Chem       Date:  2015-09-01       Impact factor: 5.157

  1 in total

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