Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB.
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.
Decanniere
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Forschungsgruppe Kristallographie, Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
Sandman
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Reeve
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Heinemann
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D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D019605:Euryarchaeota / Q000737:chemistry* / Q000235:genetics; D006657:Histones / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D006657:Histones; D011994:Recombinant Proteins; C094495:histone HMf