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Crystallization and preliminary X‐ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24
Author(s) -
Sakamoto Yasumitsu,
Suzuki Yoshiyuki,
Iizuka Ippei,
Tateoka Chika,
Roppongi Saori,
Okada Hirofumi,
aka Takamasa,
Morikawa Yasushi,
Nakamura Kazuo T.,
Ogasawara Wataru,
Tanaka Nobutada
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13034584
Subject(s) - orthorhombic crystal system , aminopeptidase , crystallography , crystallization , chemistry , resolution (logic) , crystal structure , leucine , amino acid , biochemistry , organic chemistry , artificial intelligence , computer science
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 P 2 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.