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Crystallization and preliminary X-ray diffraction studies of blasticidin S deaminase from Aspergillus terreus.

作者信息

Nakasako M, Kimura M, Yamaguchi I

机构信息

PRESTO, Japan Science and Technology Corporation and The University of Tokyo, Yayoi 1-1-1, Bunkyoku, Tokyo 113-0032, Japan.

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):547-8. doi: 10.1107/s0907444998011809.

DOI:10.1107/s0907444998011809
PMID:10089374
Abstract

Blasticidin S deaminase from Aspergillus terreus was crystallized with polyethylene glycol 8000. Two types of crystals were grown under the same crystallization conditions. One type grew as thin plates, while the other had a rhombic shape. The rhombic shaped crystal was suitable for high-resolution crystal structure analysis. Precession photographs and diffraction data showed that the crystal belonged to orthorhombic space group P212121, with unit-cell dimensions a = 70.33, b = 146.56 and c = 56.48 A. The calculated Vm value was acceptable when a tetramer of the enzyme was contained in an asymmetric unit. Preliminary diffraction data were collected to a resolution of 2.0 A with good statistics.

摘要

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