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. 2010 Jan 1;66(Pt 1):54-6.
doi: 10.1107/S1744309109048039. Epub 2009 Dec 25.

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

Young Jun An  1 , Chang-Ro Lee, Supangat Supangat, Hyun Sook Lee, Jung-Hyun Lee, Sung Gyun Kang, Sun-Shin Cha
Affiliations

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

Young Jun An et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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%.

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Figures

Figure 1
Figure 1
Crystals of TonLon.
Figure 2
Figure 2
Plot of the elution time versus the logarithm of the molecular weight of the size markers.
See this image and copyright information in PMC

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