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Digitale Medien

Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB (1996)

Decanniere, Klaas ; Sandman, Kathleen ; Reeve, John N. ; [weitere]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 24 (1996), S. 269-271

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Details

ISSN: 0887-3585

Schlagwort(e): Archaea ; hyperthermophiles ; histone fold ; X-ray diffraction ; anomalous dispersion ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: 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 P42212 and P212121. HMfB crystallized in space group P21212, while a selenomethionine-substituted variant, SeMet-HMfB, yielded crystals in C2221. In all crystal forms HMfA, HMfB, or SeMet-HMfB may be present as homodimers.

Zusätzliches Material: 3 Tab.

Materialart: Digitale Medien

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