Calmodulin, S-100, and crayfish sarcoplasmic calcium-binding protein crystals suitable for X-ray diffraction studies.
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.
D000818:Animals; D003400:Astacoidea; D001923:Brain Chemistry; D002135:Calcium-Binding Proteins / Q000302:isolation & purification; D002147:Calmodulin / Q000302:isolation & purification; D002417:Cattle; D003460:Crystallization; D009419:Nerve Tissue Proteins / Q000302:isolation & purification; D011487:Protein Conformation; D009418:S100 Proteins / Q000302:isolation & purification; D012519:Sarcoplasmic Reticulum / Q000032:analysis*; D014961:X-Ray Diffraction
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D009419:Nerve Tissue Proteins; D009418:S100 Proteins