J. Biol. Chem., Vol. 255, Issue 17, 8154-8156, 09, 1980

Calmodulin, S-100, and crayfish sarcoplasmic calcium-binding protein crystals suitable for X-ray diffraction studies

RH Kretsinger, SE Rudnick, DA Sneden and VB Schatz

We have grown crystals of calmodulin, of S-100, and crayfish sarcoplasmic calcium-binding protein and are now determining their structures by x-ray diffraction. The sarcoplasmic calcium-binding protein crystallizes from 50% 2-methyl-2,4-pentanediol in space group P2(1)2(1)2(1) with unit cell dimensions of 58.9, 68.5, and 116.1 A, and diffracts beyond 3.0 A Bragg spacing. S-100 crystallized from 15% polyethylene glycol 6000 in space group P4(1) with unit cell dimensions of 56.0, 56.0, and 112.8 A, and diffracts beyond 3.0 A. Calmodulin crystallized from 15% polyethylene glycol in space group P2(1) with unit cell dimensions of 61.8, 56.7, and 40.0 A, beta = 92.7 degrees, and diffracts beyond 5.0 A.
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