| Literature DB >> 20057071 |
Young Jun An1, Chang-Ro Lee, Supangat Supangat, Hyun Sook Lee, Jung-Hyun Lee, Sung Gyun Kang, Sun-Shin Cha.
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%.Entities:
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Year: 2009 PMID: 20057071 PMCID: PMC2805537 DOI: 10.1107/S1744309109048039
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091