CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT BOVINE NEUROCALCIN-DELTA

Neurocalcins are novel brain-specific proteins that belong to a new su bclass of the EF-hand super-family of calcium binding proteins, define d by the photoreceptor cell-specific protein recoverin (Terasawa et al ., J, Biol. Chem, 267:19596-19599, 1992), Here we report the purificat ion and crystallization of unmyristoylated recombinant bovine neurocal cin delta from Escherichia coli, Crystals of a bovine neurocalcin delt a have been grown by macro-seeding at room temperature through vapor p hase equilibration using the hanging drop technique with ammonium sulf ate as the precipitating agent. The crystals diffract to at least 2.5 BL resolution and belong to monoclinic space group P2(1) with unit cel l dimensions a = 42.734 Angstrom, b = 94.343 Angstrom, c = 50.696 Angs trom, and beta = 98.37 degrees. The asymmetric unit contains two molec ules, with corresponding crystal volume per protein mass (Vm) of 2.29 Angstrom(3)/Da and solvent fraction of 45% by volume, exhibiting an ap proximate 222 point symmetry. (C) 1996 Wiley-Liss, Inc.