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김채운

Kim, Chae Un
High Pressure X-ray Science Lab.
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dc.citation.endPage 202 -
dc.citation.number 3 -
dc.citation.startPage 194 -
dc.citation.title ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY -
dc.citation.volume 80 -
dc.contributor.author Hull, Joshua A. -
dc.contributor.author Lee, Cheol -
dc.contributor.author Kim, Jin Kyun -
dc.contributor.author Lim, Seon Woo -
dc.contributor.author Park, Jaehyun -
dc.contributor.author Park, Sehan -
dc.contributor.author Lee, Sang Jae -
dc.contributor.author Park, Gisu -
dc.contributor.author Eom, Intae -
dc.contributor.author Kim, Minseok -
dc.contributor.author Hyun, HyoJung -
dc.contributor.author Combs, Jacob E. -
dc.contributor.author Andring, Jacob T. -
dc.contributor.author Lomelino, Carrie -
dc.contributor.author Kim, Chae Un -
dc.contributor.author McKenna, Robert -
dc.date.accessioned 2024-05-16T15:05:09Z -
dc.date.available 2024-05-16T15:05:09Z -
dc.date.created 2024-05-14 -
dc.date.issued 2024-03 -
dc.description.abstract The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of 'molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO2 and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures. -
dc.identifier.bibliographicCitation ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, v.80, no.3, pp.194 - 202 -
dc.identifier.doi 10.1107/S2059798324000482 -
dc.identifier.issn 2059-7983 -
dc.identifier.scopusid 2-s2.0-85186745528 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/82638 -
dc.identifier.wosid 001206642500006 -
dc.language 영어 -
dc.publisher INT UNION CRYSTALLOGRAPHY -
dc.title XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures -
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.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor X-ray crystallography -
dc.subject.keywordAuthor NMR -
dc.subject.keywordAuthor carbonic anhydrase II -
dc.subject.keywordAuthor XFELs -
dc.subject.keywordAuthor neutron diffraction crystallography -
dc.subject.keywordAuthor radiation damage -
dc.subject.keywordPlus CRYSTALLOGRAPHY -
dc.subject.keywordPlus MECHANISM -
dc.subject.keywordPlus DIOXIDE -
dc.subject.keywordPlus RADIATION-DAMAGE -
dc.subject.keywordPlus ACTIVE-SITE -

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