S. Shima et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF FORMYLMETHANOFURAN - TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS-KANDLERI, Proteins, 26(1), 1996, pp. 118-120
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-pentamediol as prec
ipitant displayed the space group P2(1) with unit cell parameters of a
= 87.0 Angstrom, b = 75.4 Angstrom, c = 104.7 Angstrom, and beta = 11
3.9 degrees and diffracted better than 2 Angstrom 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 Angstrom and 242.1 Angs
trom. Diffraction data to 1.73 Angstrom were recorded, Crystal form S
which was crystallized from (NH4)(2)SO4 in the space group I4(1)22 wit
h unit cell parameters of 151.3 Angstrom and 249.5 Angstrom diffracted
at least to 2.2 Angstrom resolution, All crystal forms probably have
four molecules per asymmetric unit and are suitable for X-ray structur
e analysis. (C) 1996 Wiley-Liss, Inc.