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

ABSTRACT: 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 Å 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 Å. Structural analysis by the multi-wavelength anomalous diffraction method is in progress.

SUBMITTER: Sakamoto Y

PROVIDER: S-EPMC3936453 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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

Sakamoto Yasumitsu Y Suzuki Yoshiyuki Y Iizuka Ippei I Tateoka Chika C Roppongi Saori S Okada Hirofumi H Nonaka Takamasa T Morikawa Yasushi Y Nakamura Kazuo T KT Ogasawara Wataru W Tanaka Nobutada N

Acta crystallographica. Section F, Structural biology communications 20140121 Pt 2

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 Å 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 ...[more]

PMID: 24637761

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