The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

Nucleic Acids Research

Volumn 42, Issue 9, 2014, Pages 6038-6051

  Bowman, Andrew ^a   Hammond, Colin M ^a   Stirling, Andrew ^a   Ward, Richard ^a   Shang, Weifeng ^b   El Mkami, Hassane ^c   Robinson, David A ^a   Svergun, Dmitri I ^b   Norman, David G ^a   Owen Hughes, Tom ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; FUNGAL PROTEIN; NUCLEOSOME ASSEMBLY PROTEIN 1; PROTEIN VPS75; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; CELL BUDDING; CONTROLLED STUDY; CRYSTALLIZATION; ELECTRON NUCLEAR DOUBLE RESONANCE; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; YEAST;

MODELS, MOLECULAR; MOLECULAR CHAPERONES; NUCLEOSOME ASSEMBLY PROTEIN 1; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SCATTERING, SMALL ANGLE; SOLUTIONS; X-RAY DIFFRACTION;

EID: 84901332832     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku232     Document Type: Article

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