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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%.

SUBMITTER: An YJ

PROVIDER: S-EPMC2805537 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1.

An Young Jun YJ Lee Chang-Ro CR Supangat Supangat S Lee Hyun Sook HS Lee Jung-Hyun JH Kang Sung Gyun SG Cha Sun-Shin SS

Acta crystallographica. Section F, Structural biology and crystallization communications 20091225 Pt 1

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, ...[more]

PMID: 20057071

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