Preliminary crystallographic studies of the creatinine amidohydrolase from Pseudomonas putida.
Creatinine amidohydrolase (creatininase; EC 3.5.2.10) from Pseudomonas putida has been overexpressed in Escherichia coli and crystallized by the hanging-drop method. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 102.0, b = 150.7, c = 167.1 A. Native data were collected to 1.8 A resolution by a rotation method at 100 K using an ADSC Quantum 4R CCD detector with synchrotron radiation.
Ito
Kiyoshi
K
Biotechnology, Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
Kanada
Naota
N
Inoue
Takahiko
T
Furukawa
Kumiko
K
Yamashita
Kinuyo
K
Tanaka
Nobutada
N
Nakamura
Kazuo T
KT
Nishiya
Yoshiaki
Y
Sogabe
Atsushi
A
Yoshimoto
Tadashi
T
D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology*
D000581:Amidohydrolases; C019946:creatininase