Reference: Decanniere K, et al. (1996) Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB. Proteins 24(2):269-71

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Abstract


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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Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S.
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Decanniere K, Sandman K, Reeve JN, Heinemann U
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