Premium
Crystallization and preliminary X‐ray characterization of the Methanothermus fervidus histones HMfA and HMfB
Author(s) -
Decanniere Klaas,
Sandman Kathleen,
Reeve John N.,
Heinemann Udo
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199602)24:2<269::aid-prot16>3.0.co;2-l
Subject(s) - histone , crystallization , dna , nucleosome , crystallography , chemistry , biochemistry , thermophile , biology , enzyme , organic chemistry
HMfA and HMfB are histone proteins from the thermophilic archaeon Methanothermus fervidus . They wrap DNA into nucleosome‐like structures and appear to represent the basic core histone fold. HMfA was crystallized in space groups P4 2 2 1 2 and P2 1 2 1 2 1 . HMfB crystallized in space group P2 1 2 1 2, while a selenomethionine‐substituted variant, SeMet‐HMfB, yielded crystals in C222 1 . In all crystal forms HMfA, HMfB, or SeMet‐HMfB may be present as homodimers.