Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8.
Peptide deformylase (PDF) is responsible for cleaving the formyl group at the N-terminus of nascent polypeptide chains in eubacteria and is essential to bacterial cell viability. A recombinant PDF of the thermophilic bacterium Thermus thermophilus HB8 has been crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystals belonged to the tetragonal space group P4(1) or P4(3), with unit-cell parameters a = b = 62.58, c = 105.27 A, and are most likely to contain two molecules in an asymmetric unit, giving a crystal volume per protein weight (V(M)) of 2.3 A(3) Da(-1) and a solvent content of 46.7%.
Kamo
Masayuki
M
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Kudo
Norio
N
Lee
Woo Cheol
WC
Motoshima
Hiroyuki
H
Tanokura
Masaru
M
D000581:Amidohydrolases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016963:Thermus thermophilus / Q000201:enzymology*
D000581:Amidohydrolases; C084507:peptide deformylase