CRYSTALLIZATION AND PRELIMINARY-X-RAY CHARACTERIZATION OF THE METHANOTHERMUS-FERVIDUS HISTONES HMFA AND HMFB

Citation
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
Citations number
19
Categorie Soggetti
Biology
Journal title
ISSN journal
08873585
Volume
24
Issue
2
Year of publication
1996
Pages
269 - 271
Database
ISI
SICI code
0887-3585(1996)24:2<269:CAPCOT>2.0.ZU;2-T
Abstract
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.