Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1.
Lon is an oligomeric ATP-dependent protease that degrades defective or denatured proteins as well as some folded proteins for the control of cellular protein quality and metabolism. Lon from Thermococcus onnurineus NA1 was purified and crystallized at 295 K. A 2.0 A resolution data set was collected using synchrotron radiation. The crystals belonged to space group P6(3), with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 A. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.
An
Young Jun
YJ
Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan 426-744, Republic of Korea.
Lee
Chang-Ro
CR
Supangat
Supangat
S
Lee
Hyun Sook
HS
Lee
Jung-Hyun
JH
Kang
Sung Gyun
SG
Cha
Sun-Shin
SS
D003460:Crystallization; D018360:Crystallography, X-Ray; D049070:Protease La / Q000737:chemistry*; D019712:Thermococcus / Q000201:enzymology
D049070:Protease La