Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1 SCIE SCOPUS
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | An, Young Jun | - |
| dc.contributor.author | Lee, Chang-Ro | - |
| dc.contributor.author | Supangat, Supangat | - |
| dc.contributor.author | Lee, Hyun Sook | - |
| dc.contributor.author | Lee, Jung-Hyun | - |
| dc.contributor.author | Kang, Sung Gyun | - |
| dc.contributor.author | Cha, Sun-Shin | - |
| dc.date.accessioned | 2020-04-20T08:55:16Z | - |
| dc.date.available | 2020-04-20T08:55:16Z | - |
| dc.date.created | 2020-01-28 | - |
| dc.date.issued | 2010-01 | - |
| dc.identifier.issn | 1744-3091 | - |
| dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/4149 | - |
| 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 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%. | - |
| dc.description.uri | 1 | - |
| dc.language | English | - |
| dc.publisher | INT UNION CRYSTALLOGRAPHY | - |
| dc.title | Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1 | - |
| dc.type | Article | - |
| dc.citation.endPage | 56 | - |
| dc.citation.startPage | 54 | - |
| dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
| dc.citation.volume | 66 | - |
| dc.contributor.alternativeName | 안영준 | - |
| dc.contributor.alternativeName | Supangat | - |
| dc.contributor.alternativeName | 이현숙 | - |
| dc.contributor.alternativeName | 이정현 | - |
| dc.contributor.alternativeName | 강성균 | - |
| dc.contributor.alternativeName | 차선신 | - |
| dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.66, pp.54 - 56 | - |
| dc.identifier.doi | 10.1107/S1744309109048039 | - |
| dc.identifier.scopusid | 2-s2.0-75149160444 | - |
| dc.identifier.wosid | 000273072500016 | - |
| dc.type.docType | Article | - |
| dc.description.journalClass | 1 | - |
| dc.description.isOpenAccess | N | - |
| dc.subject.keywordPlus | ATP-DEPENDENT PROTEASE | - |
| dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
| dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
| dc.subject.keywordPlus | PROTEOLYTIC DOMAIN | - |
| dc.subject.keywordPlus | QUALITY-CONTROL | - |
| dc.subject.keywordPlus | ACTIVE-SITE | - |
| dc.subject.keywordPlus | RESOLUTION | - |
| dc.subject.keywordPlus | BACTERIAL | - |
| dc.subject.keywordPlus | PROTEINS | - |
| dc.subject.keywordPlus | REVEALS | - |
| dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
| dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
| dc.relation.journalWebOfScienceCategory | Biophysics | - |
| dc.relation.journalWebOfScienceCategory | Crystallography | - |
| dc.description.journalRegisteredClass | scie | - |
| dc.description.journalRegisteredClass | scopus | - |
| dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
| dc.relation.journalResearchArea | Biophysics | - |
| dc.relation.journalResearchArea | Crystallography | - |
- Appears in Collections:
- Marine Resources & Environment Research Division > Marine Biotechnology &Bioresource Research Department > 1. Journal Articles
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