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Crystallization and preliminary X‐ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis
Author(s) -
Sakamoto Yasumitsu,
Suzuki Yoshiyuki,
Iizuka Ippei,
Tateoka Chika,
Roppongi Saori,
Fujimoto Mayu,
Gouda Hiroaki,
aka Takamasa,
Ogasawara Wataru,
Tanaka Nobutada
Publication year - 2015
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/s2053230x15000424
Subject(s) - orthorhombic crystal system , porphyromonas gingivalis , dipeptidyl peptidase , crystallography , crystallization , resolution (logic) , escherichia coli , chemistry , x ray crystallography , materials science , diffraction , crystal structure , enzyme , bacteria , biology , biochemistry , optics , physics , organic chemistry , artificial intelligence , computer science , gene , genetics
Dipeptidyl peptidase 11 from Porphyromonas gingivalis (PgDPP11) preferentially cleaves substrate peptides with Asp and Glu at the P1 position [NH 2 –P2–P1(Asp/Glu)–P1′–P2′…]. For crystallographic studies, PgDPP11 was overproduced in Escherichia coli , purified and crystallized using the hanging‐drop vapour‐diffusion method. X‐ray diffraction data to 1.82 Å resolution were collected from an orthorhombic crystal form belonging to space group C 222 1 , with unit‐cell parameters a = 99.33, b = 103.60, c = 177.33 Å. Structural analysis by the multi‐wavelength anomalous diffraction method is in progress.