K. Decanniere et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY CHARACTERIZATION OF THE METHANOTHERMUS-FERVIDUS HISTONES HMFA AND HMFB, Proteins, 24(2), 1996, pp. 269-271
HMfA and HMfB are histone proteins from the thermophilic archaeon Meth
anothermus fervidus, They wrap DNA into nucleosome-like structures and
appear to represent the basic core histone fold, HMfA was crystallize
d in space groups P4(2)2(1)2 and P2(1)2(1)2(1). HMfB crystallized in s
pace group P2(1)2(1)2, while a selenomethionine-substituted variant, S
eMet-HMfB, yielded crystals in C222(1). In all crystal forms HMfA, HMf
B, or SeMet-HMfB may be present as homodimers. (C) 1996 Wiley-Liss, In
c.