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 , with unitcell parameters a = 121.45, b = 121.45, c = 195.24 A 54 doi:10.1107/S1744309109048039 Acta Cryst. (2010). F66, 54–56 3 ˚ . Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.