Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom.
Cysteine-rich secretory proteins (CRISPs) play an important role in the innate immune system and are transcriptionally regulated by androgens in several tissues. The proteins are mostly found in the epididymis and granules of mammals, whilst a number of snake venoms also contain CRISP-family proteins. The natrin protein from the venom of Naja atra (Taiwan cobra), which belongs to a family of CRISPs and has a cysteine-rich C-terminal amino-acid sequence, has been purified using a three-stage chromatography procedure and crystals suitable for X-ray analysis have been obtained using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.58 A resolution using synchrotron radiation; the crystals belong to space group C222(1), with unit-cell parameters a = 59.172, b = 65.038, c = 243.156 A. There are two protein molecules in the asymmetric unit and the Matthews coefficient is estimated to be 2.35 A3 Da(-1), corresponding to a solvent content of 47.60%.
Wang
Yu-Ling
YL
Biology Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30077, Taiwan.
Goh
King-Xiang
KX
Wu
Wen-guey
WG
Chen
Chun-Jung
CJ
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry*; D004546:Elapid Venoms; D017815:Elapidae; D008562:Membrane Glycoproteins / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D004546:Elapid Venoms; D008562:Membrane Glycoproteins; D011506:Proteins; D003545:Cysteine