The BioGRID | PUBLICATION VIEW

	Proteins Jul (1995); 22(3):293-7
Crystallization and preliminary X-ray analysis of the cytoplasmic domain of human erythrocyte band 3.
Kiyatkin AB, Natarajan P, Munshi S, Minor W, Johnson JE, Low PS
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-1393, USA.
Abstract: A cytoplasmic domain of the human erythrocyte membrane protein band 3 (M(r) = 42,500), residues 1-379, expressed in and purified from E. coli, has been crystallized by the method of vapor diffusion in sitting drops with subsequent streak-seeding at room temperature. Initial crystals were grown from solutions containing 65-68% saturated ammonium sulfate at pH 4.9 and 2 mg/ml protein. Subsequent streak-seeding into solutions of 50-53% ammonium sulfate at pH 4.9 and 7 mg/ml protein produced single crystals suitable for X-ray analysis, which contained pure protein as revealed by gel electrophoresis. The crystals belong to the monoclinic space group C2 with cell dimensions of a = 178.8 A, b = 90.5 A, c = 122.1 A, and beta = 131.3 degrees and diffract at least to 2.7 A resolution (at 100 K). A self-rotation function shows the presence of approximate 222 local symmetry.
[PUBMED: 7479704]