Full metadata record

DC Field Value Language
dc.contributor.authorYang, JK-
dc.contributor.authorChang, CS-
dc.contributor.authorCho, SJ-
dc.contributor.authorLee, JY-
dc.contributor.authorYu, YG-
dc.contributor.authorEom, SH-
dc.contributor.authorSuh, SW-
dc.date.accessioned2024-01-21T09:12:29Z-
dc.date.available2024-01-21T09:12:29Z-
dc.date.created2021-09-03-
dc.date.issued2003-03-
dc.identifier.issn0907-4449-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/138789-
dc.description.abstractA putative aspartate aminotransferase from the hyperthermophilic archaeon Methanococcus jannaschii encoded by the Mj0684 gene has been overexpressed in Escherichia coli and crystallized at 296 Kusing the sitting-drop vapour-diffusion method. The crystals belong to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 111.87, c = 60.86 Angstrom. They diffract to 2.2 Angstrom resolution using Cu Kalpha X-rays. The asymmetric unit contains a single subunit of the recombinant Mj0684 gene product, giving a corresponding V-M of 2.25 Angstrom(3) Da(-1) and a solvent content of 45.3% by volume. An X-ray diffraction data set has been collected to 2.2 Angstrom at 295 K.-
dc.languageEnglish-
dc.publisherBLACKWELL MUNKSGAARD-
dc.subjectTHERMUS-THERMOPHILUS HB8-
dc.subjectCRYSTAL-STRUCTURE-
dc.subjectSUBSTRATE-SPECIFICITY-
dc.subjectREFINEMENT-
dc.subjectPROTEINS-
dc.subjectCOMPLEX-
dc.subjectFORMS-
dc.subjectMODE-
dc.titleCrystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii-
dc.typeArticle-
dc.identifier.doi10.1107/S0907444903000076-
dc.description.journalClass1-
dc.identifier.bibliographicCitationACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.59, pp.563 - 565-
dc.citation.titleACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY-
dc.citation.volume59-
dc.citation.startPage563-
dc.citation.endPage565-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000181609800032-
dc.identifier.scopusid2-s2.0-0037348392-
dc.relation.journalWebOfScienceCategoryBiochemical Research Methods-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalWebOfScienceCategoryCrystallography-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalResearchAreaCrystallography-
dc.type.docTypeArticle-
dc.subject.keywordPlusTHERMUS-THERMOPHILUS HB8-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusSUBSTRATE-SPECIFICITY-
dc.subject.keywordPlusREFINEMENT-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusFORMS-
dc.subject.keywordPlusMODE-
dc.subject.keywordAuthorcrystal-
dc.subject.keywordAuthoraminotransferase-
dc.subject.keywordAuthormethanoccous jannaschii-
Appears in Collections:
KIST Article > 2003
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE