Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus.
Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 A resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 171.0, b = 231.6, c = 124.9 A. The crystal contains three molecules in an asymmetric unit (VM = 2.11 A3 Da(-1)) and has a solvent content of 61.5%.
Nagata
Koji
K
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, 113-8657, Japan.
Tsutsui
Shiho
S
Lee
Woo Cheol
WC
Ito
Kosuke
K
Kamo
Masayuki
M
Inoue
Yumiko
Y
Tanokura
Masaru
M
D002268:Carboxypeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D013050:Spectrometry, Fluorescence; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics
D002268:Carboxypeptidases