| dc.contributor.author | Young Jun An | |
| dc.contributor.author | Chang-Ro Lee | |
| dc.contributor.author | Supangat, Supangat | |
| dc.contributor.author | Hyun Sook Lee | |
| dc.contributor.author | Jung-Hyun Lee | |
| dc.contributor.author | Sung Gyun Kang | |
| dc.contributor.author | Sun-Shin Cha | |
| dc.date.accessioned | 2019-07-26T05:45:34Z | |
| dc.date.available | 2019-07-26T05:45:34Z | |
| dc.date.issued | 2019-07-26 | |
| dc.identifier.issn | 1744-3091 | |
| dc.identifier.uri | http://repository.unej.ac.id/handle/123456789/91391 | |
| dc.description | Acta Crystallographica Section F (Structural Biology and Crystallization Communications), Vol. 66, Issue 1, January 2010 | en_US |
| dc.description.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%. | en_US |
| dc.language.iso | en | en_US |
| dc.subject | Crystallization | en_US |
| dc.subject | preliminary X-ray | en_US |
| dc.subject | crystallographic | en_US |
| dc.subject | Thermococcus onnurineus | en_US |
| dc.subject | NA1 | en_US |
| dc.title | Crystallization and Preliminary X-ray Crystallographic Analysis of Lon from Thermococcus onnurineus NA1 | en_US |
| dc.type | Article | en_US |
