Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24

被引：4

作者：

Sakamoto, Yasumitsu ^{[1
]}

Suzuki, Yoshiyuki ^{[2
]}

Iizuka, Ippei ^{[1
]}

Tateoka, Chika ^{[1
]}

Roppongi, Saori ^{[1
]}

Okada, Hirofumi ^{[2
]}

Nonaka, Takamasa ^{[1
]}

Morikawa, Yasushi ^{[2
]}

Nakamura, Kazuo T. ^{[3
]}

Ogasawara, Wataru ^{[2
]}

Tanaka, Nobutada ^{[3
]}

机构：

[1] Iwate Med Univ, Sch Pharm, Yahaba, Iwate 0283694, Japan

[2] Nagaoka Univ Technol, Dept Bioengn, Nagaoka, Niigata 9402188, Japan

[3] Showa Univ, Sch Pharm, Shinagawa Ku, Tokyo 1428555, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

关键词：

PSEUDOMONAS-SP WO24; CRYSTAL-STRUCTURE; IV; EXPRESSION; GENE;

D O I：

10.1107/S2053230X13034584

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24 (DAP BII) is able to cleave a variety of dipeptides from the amino-terminus of substrate peptides. For crystallographic studies, DAP BII was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 2.3 angstrom resolution were collected using an orthorhombic crystal form belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.55, b = 130.86, c = 170.87 angstrom. Structural analysis by the multi-wavelength anomalous diffraction method is in progress.

引用

页码：221 / 224

页数：4

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