Crystallization of Clonorchis sinensis 26 kDa glutathione S-transferase and its fusion proteins with peptides of different lengths
DC Field | Value | Language |
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dc.contributor.author | Han, YH | - |
dc.contributor.author | Chung, YH | - |
dc.contributor.author | Kim, TY | - |
dc.contributor.author | Hong, SJ | - |
dc.contributor.author | Choi, JD | - |
dc.contributor.author | Chung, YJ | - |
dc.date.available | 2019-05-30T09:40:08Z | - |
dc.date.issued | 2001-04 | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/25234 | - |
dc.description.abstract | A Clonorchis sinensis 26 kDa glutathione S-transferase (CsGST) and its fusion proteins containing 14 and 48 amino-acid peptides at the N-terminus have been crystallized using polyethylene glycol monomethylether 550 as a precipitant. Crystals of the three proteins show very similar crystal properties: they diffract to at least 2.3 Angstrom resolution and belong to the orthorhombic space group P2(1)2(1)2(1). The unit-cell parameters of CsGST crystals were a = 66.64 (1), b = 68.91 (1), c = 123.41 (2) Angstrom, which are very close to those of the crystals of the two fusion proteins. In addition, CsGST fusion proteins containing varying extents of N-terminal-extended peptides are incorporated into a crystal, indicating that the extended peptides have little effect on crystal packing. These results suggest that the crystallization system of CsGST/peptide fusion protein may be generally applicable to obtain crystals of small peptides. | - |
dc.format.extent | 3 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | MUNKSGAARD INT PUBL LTD | - |
dc.title | Crystallization of Clonorchis sinensis 26 kDa glutathione S-transferase and its fusion proteins with peptides of different lengths | - |
dc.type | Article | - |
dc.identifier.doi | 10.1107/S0907444900019314 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.57, pp 579 - 581 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000167663500014 | - |
dc.identifier.scopusid | 2-s2.0-0035075308 | - |
dc.citation.endPage | 581 | - |
dc.citation.startPage | 579 | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | - |
dc.citation.volume | 57 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordPlus | BINDING DOMAIN | - |
dc.subject.keywordPlus | VACCINE | - |
dc.subject.keywordPlus | ISOENZYMES | - |
dc.subject.keywordPlus | DRUG | - |
dc.subject.keywordPlus | GST | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |
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 | - |
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