Crystallization and preliminary X-ray crystallographic studies of recombinant bovine neurocalcin delta

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