The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer

Biochemical and Biophysical Research Communications

Volumn 315, Issue 1, 2004, Pages 10-15

  Nakamura, Akira ^a   Komori, Hirofumi ^a,c   Kobayashi, Gengo ^a   Kita, Akiko ^a   Wada, Chieko ^a   Miki, Kunio ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b RIKEN Harima Institute/SPring 8 ^*  (Japan)

^c STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Crystallization; Dimerization domain; DnaK chaperone; Mini F plasmid; RepE; Replication initiator

Indexed keywords

CHAPERONE; DIMER; MONOMER; PROTEIN; REPLICATION INITIATOR PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CROSS LINKING; CRYSTALLIZATION; DIMERIZATION; GEL FILTRATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REGULATORY MECHANISM; ULTRACENTRIFUGATION; WILD TYPE;

ESCHERICHIA COLI;

EID: 0842308122     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.01.018     Document Type: Article

References (15)

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