Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB.

Proteins

Forschungsgruppe Kristallographie, Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.

Published: February 1996

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.

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http://dx.doi.org/10.1002/(SICI)1097-0134(199602)24:2<269::AID-PROT16>3.0.CO;2-LDOI Listing

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