Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule.
A hybrid molecule consisting of calmodulin (CaM) and the CaM-binding domain of olfactory nucleotide-gated ion-channel peptide (CaM-OLFp) was purified and crystallized by the hanging-drop vapour-diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 A at cryogenic temperature (100 K) using X-rays from a rotating anode (Cu, wavelength 1.54 A). The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 64.76, b = 36.23, c = 70.96 A, alpha = gamma = 90, beta = 109.4 degrees. Analysis of the packing density shows that the asymmetric unit contains one CaM-OLFp hybrid molecule with a solvent content of 36.42%.
Chyan
Chia-Lin
CL
Department of Chemistry, National Dong-Hwa University, Hualien 974, Taiwan. chyan@mail.ndhu.edu.tw
Huang
Po-Chung
PC
Lin
Ta-Hsien
TH
Huang
Jian-Wen
JW
Lin
S S
SS
Huang
Hsien-bin
HB
Chen
Yi-Cheng
YC
D000818:Animals; D002147:Calmodulin / Q000737:chemistry*; D002645:Chickens; D003460:Crystallization; D018360:Crystallography, X-Ray; D054815:Cyclic Nucleotide-Gated Cation Channels; D007473:Ion Channels / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
D002147:Calmodulin; D054815:Cyclic Nucleotide-Gated Cation Channels; D007473:Ion Channels; D011993:Recombinant Fusion Proteins