There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 1627 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 1624 | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS | - |
dc.citation.volume | 70 | - |
dc.contributor.author | Jeong, Hanbin | - |
dc.contributor.author | Lee, Hakbong | - |
dc.contributor.author | Lee, Changwook | - |
dc.date.accessioned | 2023-12-22T01:48:56Z | - |
dc.date.available | 2023-12-22T01:48:56Z | - |
dc.date.created | 2015-01-02 | - |
dc.date.issued | 2014-12 | - |
dc.description.abstract | Terminally misfolded or unassembled proteins are selectively recognized and cleared by the ER-associated degradation (ERAD) pathway. Suppressor/enhancer of lin-12-like (SEL1L), a component of the dislocation machinery containing the E3 ubiquitin ligase Hrd1, plays an important role in selecting and transporting ERAD substrates for degradation in the endoplasmic reticulum. In this study, the purification, crystallization and preliminary X-ray diffraction analysis of recombinant mouse SEL1L (residues 348-533) are reported. The crystals were obtained by the hanging-drop vapour-diffusion method at pH 8.5 and 277 K using 30% 2-propanol as a precipitant. Optimized crystals diffracted to 3.3 angstrom resolution at a synchrotron-radiation source. Preliminary X-ray diffraction analysis revealed that the crystals belonged to space group P2(1) and contained four molecules per asymmetric unit, with a solvent content of 44%. | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.70, no.12, pp.1624 - 1627 | - |
dc.identifier.doi | 10.1107/S2053230X14023115 | - |
dc.identifier.issn | 2053-230X | - |
dc.identifier.scopusid | 2-s2.0-84925883649 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/9786 | - |
dc.identifier.url | http://scripts.iucr.org/cgi-bin/paper?S2053230X14023115 | - |
dc.identifier.wosid | 000345843300011 | - |
dc.language | 영어 | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.title | Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Biophysics; Crystallography | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | TPR | - |
dc.subject.keywordPlus | RETICULUM-ASSOCIATED DEGRADATION | - |
dc.subject.keywordPlus | ENDOPLASMIC-RETICULUM | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | UBIQUITIN | - |
dc.subject.keywordPlus | TRANSLOCATION | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | FOLD | - |
dc.subject.keywordPlus | ERAD | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.