Crystallization and preliminary X-ray diffraction studies of perchloric acid soluble protein (PSP) from rat liver

Perchloric acid soluble protein purified from the cytosol fraction of rat liver has been crystallized in a form suitable for high-resolution X-ray diffraction studies. Octahedral crystals reaching 0.5 mm in cross-sectional diameter were produced by the hanging-drop method using polyethylene glycol (M-r = 8 kDa) as precipitant. These crystals diffract to 2.44 Angstrom on an in-house X-ray source and to 1.8 Angstrom using a bending-magnet beamline at ESRF Grenoble. The crystals belong to the cubic space group P2(1)3 with a = 89.90 Angstrom and two molecules per asymmetric unit, as indicated from a V-m value of 2.12 Angstrom Da(-1) and self-rotation function computation. Screening for heavy-atom derivatives identified a platinum compound and xenon that bind to the protein.