Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1
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Title
- Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1
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Author(s)
- An, Young Jun; Lee, Chang-Ro; Supangat, Supangat; Lee, Hyun Sook; Lee, Jung-Hyun; Kang, Sung Gyun; Cha, Sun-Shin
- KIOST Author(s)
- An, Young Jun(안영준); Lee, Hyun Sook(이현숙); Lee, Jung Hyun(이정현); Kang, Sung Gyun(강성균)
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Alternative Author(s)
- 안영준; Supangat; 이현숙; 이정현; 강성균; 차선신
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Publication Year
- 2010-01
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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 angstrom 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 angstrom. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.
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ISSN
- 1744-3091
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/4149
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DOI
- 10.1107/S1744309109048039
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Bibliographic Citation
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.66, pp.54 - 56, 2010
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Publisher
- INT UNION CRYSTALLOGRAPHY
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Type
- Article
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Language
- English
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Document Type
- Article
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