Crystallization and preliminary X-ray diffraction analysis of creatine amidinohydrolase from Actinobacillus.
The homodimeric form of creatine amidinohydrolase from Actinobacillus has been crystallized by the hanging-drop vapour-diffusion method followed by macroseeding using PEG 6000 as a precipitant. The crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. A complete diffraction data set using synchrotron radiation was collected to 2.7 A resolution.
Padmanabhan
Balasundaram
B
Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), 5-9-6 Tokodai, Tsukuba, Ibaraki 300-2635, Japan.
Horikoshi
Masami
M
D000188:Actinobacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D014512:Ureohydrolases / Q000737:chemistry* / Q000378:metabolism
D014512:Ureohydrolases; C019944:creatinase