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Crystallization and preliminary x‐ray crystallographic studies of recombinant bovine neurocalcin δ
Author(s) -
Kumar Vinod D.,
Hidaka Hiroyoshi,
Okazaki Katsuo,
VijayKumar Senadhi
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199606)25:2<261::aid-prot11>3.0.co;2-h
Subject(s) - crystallization , crystallography , recombinant dna , ammonium sulfate , chemistry , monoclinic crystal system , protein crystallization , crystal structure , chromatography , biochemistry , organic chemistry , gene
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 δ from Escherichia coli . Crystals of a bovine neurocalcin δ 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 Å resolution and belong to monoclinic space group P2 I with unit cell dimensions a = 42.734 Å, b = 94.343 Å, c = 50.696 Å, and β = 98.37°. The asymmetric unit contains two molecules, with corresponding crystal volume per protein mass (Vm) of 2.29 Å 3 /Da and solvent fraction of 45% by volume, exhibiting an approximate 222 point symmetry. © 1996 Wiley‐Liss, Inc.