The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold

Proteins: Structure, Function and Genetics

Volumn 62, Issue 1, 2006, Pages 8-16

  Qiu, Yang ^a   Tereshko, Valentine ^a   Kim, Youngchang ^b   Zhang, Rongguang ^b   Collart, Frank ^b   Yousef, Mohammed ^a   Kossiakoff, Anthony ^a   Joachimink, Andrzej ^a,b  

^a UNIVERSITY OF CHICAGO   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Histone fold; MAD phasing; Structural genomics; Synchrotron radiation; Thermostability

Indexed keywords

BACTERIAL PROTEIN; HISTONE; MONOMER; PROTEIN AQ 328; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AQUIFEX AEOLICUS; ARTICLE; CRYSTAL STRUCTURE; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEDIMENTATION; TANDEM REPEAT; THERMOSTABILITY;

BACTERIA; BACTERIAL PROTEINS; CLONING, MOLECULAR; CRYSTALLIZATION; CRYSTALLOGRAPHY; ESCHERICHIA COLI; HISTONES; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

AQUIFEX AEOLICUS; ARCHAEA; BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 30344469374     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20590     Document Type: Article

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