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

Young Jun An; Chang Ro Lee; Supangat Supangat; Hyun Sook Lee; Jung Hyun Lee; Sung Gyun Kang; Sun Shin Cha

doi:10.1107/S1744309109048039

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

Young Jun An, Chang Ro Lee, Supangat Supangat, Hyun Sook Lee, Jung Hyun Lee, Sung Gyun Kang, Sun Shin Cha

Department of Chemistry & Nanoscience

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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 Å resolution data set was collected using synchrotron radiation. The crystals belonged to space group P6₃, with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 Å. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.

Original language	English
Pages (from-to)	54-56
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	1
DOIs	https://doi.org/10.1107/S1744309109048039
State	Published - 25 Dec 2009

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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 {\AA} resolution data set was collected using synchrotron radiation. The crystals belonged to space group P63, with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 {\AA}. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.",

author = "An, {Young Jun} and Lee, {Chang Ro} and Supangat Supangat and Lee, {Hyun Sook} and Lee, {Jung Hyun} and Kang, {Sung Gyun} and Cha, {Sun Shin}",

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doi = "10.1107/S1744309109048039",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1

AU - An, Young Jun

AU - Lee, Chang Ro

AU - Supangat, Supangat

AU - Lee, Hyun Sook

AU - Lee, Jung Hyun

AU - Kang, Sung Gyun

AU - Cha, Sun Shin

PY - 2009/12/25

Y1 - 2009/12/25

N2 - 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 Å resolution data set was collected using synchrotron radiation. The crystals belonged to space group P63, with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 Å. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.

AB - 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 Å resolution data set was collected using synchrotron radiation. The crystals belonged to space group P63, with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 Å. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.

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SN - 1744-3091

VL - 66

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EP - 56

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 1

ER -

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

Abstract

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