Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri.
Formylmethanofuran:tetrahydromethanopterin formyltransferase from the hyperthermophilic methanogenic Archaeon Methanopyrus kandleri (growth temperature optimum 98 degrees C) was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as precipitant displayed the space group P2(1) with unit cell parameters of a = 87.0 A, b = 75.4 A, c = 104.7 A, and beta = 113.9 degrees and diffracted better than 2 A resolution. Crystal form P grown from polyethylene glycol 8000 belonged to the space group I4(1)22 and had unit cell parameters of 157.5 A and 242.1 A. Diffraction data to 1.73 A were recorded. Crystal form S which was crystallized from (NH4)2SO4 in the space group I4(1)22 with unit cell parameters of 151.3 A and 249.5 A diffracted at least to 2.2 A resolution. All crystal forms probably have four molecules per asymmetric unit and are suitable for X-ray structure analysis.
Shima
S
S
Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Philipps-Universität, Marburg, Germany.
Thauer
R K
RK
Michel
H
H
Ermler
U
U
D001105:Archaea / Q000201:enzymology*; D003460:Crystallization; D003461:Crystallography; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D019877:Hydroxymethyl and Formyl Transferases; D013696:Temperature; D014166:Transferases / Q000737:chemistry*
D014166:Transferases; D019877:Hydroxymethyl and Formyl Transferases; C050840:formylmethanofuran-tetrahydromethanopterin formyltransferase