Abstract
Breast cancer metastasis suppressor 1 (BRMS1) is an inhibitor of metastatic progression and plays a role in several steps of the metastatic cascade. Apart from the ability of BRMS1 to negatively regulate metastasis formation in breast, melanoma and ovarian tumours, very little is known about the molecular aspects of the antimetastatic properties of BRMS1. Here, the expression, purification and crystallization of a functional fragment of human BRMS1 that is predicted to be a coiled-coil region are reported. The purified fragment crystallized in space group C222(1) using the vapour-diffusion method. The unit-cell parameters were a = 42.6, b = 191.3, c = 71.9 A. The crystals diffracted to 2.0 A resolution and a complete data set was collected under cryoconditions. This is the first structural report of BRMS1.