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Crystallization and preliminary x‐ray crystallographic studies of recombinant bovine neurocalcin δ

✍ Scribed by Kumar, Vinod D.; Hidaka, Hiroyoshi; Okazaki, Katsuo; Vijay‐Kumar, Senadhi

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
459 KB
Volume
25
Category
Article
ISSN
0887-3585

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✦ Synopsis

Neurocalcins are novel brainspecific 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. 267:1959619599, 1992). Here we report the purification and crystallization of unmyristoylated recombinant bovine neurocalcin 6 from Escherichia coli. Crystals of a bovine neurocalcin 6 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 A resolution and belong to monoclinic space group P2, with unit cell dimensions a = 42.734 A, b = 94.343 A, c = 50.696 A, and f3 = 98.37'. The asymmetric unit contains two molecules, with corresponding crystal volume per protein mass (Vm) of 2.29 A3/Da and solvent fraction of 45% by volume, exhibiting an approximate 222 point symmetry. o 19% Wiley-Liss, he.

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