Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis.
A recombinant form of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis has been crystallized by the hanging-drop vapour-diffusion method using potassium sodium tartrate as a precipitating agent. The crystals belong to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 149.4, c = 159.7 A. The crystals are most likely to contain one subunit of a dimer in the asymmetric unit, with a VM value of 3.14 A3 Da(-1). Diffraction data were collected to 2.1 A resolution using synchrotron radiation at the BL5 station of the Photon Factory.
Nakajima
Yoshitaka
Y
Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Ito
Kiyoshi
K
Xu
Yue
Y
Yamada
Nozomi
N
Onohara
Yuko
Y
Ito
Takashi
T
Yoshimoto
Tadashi
T
D001426:Bacterial Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D004926:Escherichia coli / Q000378:metabolism; D016366:Open Reading Frames; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000737:chemistry*; D017356:Synchrotrons
D001426:Bacterial Proteins; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C118449:PtpA protein, Porphyromonas gingivalis; D012697:Serine Endopeptidases