Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 63, Issue -, Pages 613-615Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309107028473
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BRD2 is a bromodomain-containing BET-family protein that associates with acetylated histones throughout the cell cycle. Although the tertiary structures of the bromodomains involved in histone acetyl transfer are already known, the structures of the BET-type bromodomains, which are required for tight association with acetylated chromatin, are poorly understood. Here, the expression, purification and crystallization of the C-terminal bromodomain of human BRD2 are reported. The protein was crystallized by the sitting-drop vapour-diffusion method in the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 71.78, b = 52.60, c = 32.06 angstrom and one molecule per asymmetric unit. The crystal diffracted beyond 1.80 angstrom resolution using synchrotron radiation.
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