Purification, crystallization and preliminary X-ray diffraction of the C-terminal bromodomain from human BRD2.

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 A and one molecule per asymmetric unit. The crystal diffracted beyond 1.80 A resolution using synchrotron radiation.