Crystallization and Preliminary X-ray Crystallographic Analysis of Lon from Thermococcus onnurineus NA1

Please use this identifier to cite or link to this item: https://repository.unej.ac.id/xmlui/handle/123456789/91391

Title:	Crystallization and Preliminary X-ray Crystallographic Analysis of Lon from Thermococcus onnurineus NA1
Authors:	Young Jun An Chang-Ro Lee Supangat, Supangat Hyun Sook Lee Jung-Hyun Lee Sung Gyun Kang Sun-Shin Cha
Keywords:	Crystallization preliminary X-ray crystallographic Thermococcus onnurineus NA1
Issue Date:	26-Jul-2019
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%.
Description:	Acta Crystallographica Section F (Structural Biology and Crystallization Communications), Vol. 66, Issue 1, January 2010
URI:	http://repository.unej.ac.id/handle/123456789/91391
ISSN:	1744-3091
Appears in Collections:	LSP-Jurnal Ilmiah Dosen

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