title: Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1.
abstract: 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%.
authors.affiliation: Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan 426-744, Republic of Korea.
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: An
authors.forename: Chang-Ro
authors.initials: CR
authors.lastname: Lee
authors.forename: Supangat
authors.initials: S
authors.lastname: Supangat
authors.forename: Hyun Sook
authors.initials: HS
authors.lastname: Lee
authors.forename: Jung-Hyun
authors.initials: JH
authors.lastname: Lee
authors.forename: Sung Gyun
authors.initials: SG
authors.lastname: Kang
authors.forename: Sun-Shin
authors.initials: SS
authors.lastname: Cha
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D049070:Protease La / Q000737:chemistry*; D019712:Thermococcus / Q000201:enzymology
chemical_list: D049070:Protease La