ISSN:
0887-3585
Keywords:
X-ray diffraction
;
calcium-binding myristoylation
;
noncrystallographic symmetry
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
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 P2I 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 Å3/Da and solvent fraction of 45% by volume, exhibiting an approximate 222 point symmetry. © 1996 Wiley-Liss, Inc.
Additional Material:
1 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/prot.11
Permalink
