Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1
DC Field | Value | Language |
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dc.contributor.author | Park, Sang Ho | - |
dc.contributor.author | Chung, Ho Kyung | - |
dc.contributor.author | Kim, Do Jin | - |
dc.contributor.author | Han, Mi Ra | - |
dc.contributor.author | Park, Mi Seul | - |
dc.contributor.author | Oh, Uhtaek | - |
dc.contributor.author | Kim, Hyun-Jung | - |
dc.contributor.author | Han, Byung Woo | - |
dc.date.available | 2019-05-29T11:35:07Z | - |
dc.date.issued | 2011-10 | - |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.issn | 2053-230X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21237 | - |
dc.description.abstract | Transmembrane protein 16A (TMEM16A, also known as anoctamin 1; ANO1) is a bona fide Ca2+-activated chloride channel that is activated by intracellular Ca2+- and Ca2+-mobilizing stimuli and plays important roles in a variety of physiological functions. To elucidate the structural features of ANO1, structural analysis of the C-terminal cytosolic domain of mouse ANO1 (mANO1-CTD) was initiated. mANO1-CTD was overexpressed in Escherichia coli and was crystallized at 297 K using a reservoir solution consisting of 0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl pH 8.5 and 30%(w/v) PEG 4000. X-ray diffraction data were collected to 2.3 angstrom resolution. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 73.96, b = 103.73, c = 114.71 angstrom. If it is assumed that eight copies of a monomer molecule are present in the crystallographic asymmetric unit, the crystal volume per protein mass (V-M) is 2.38 angstrom(3) Da(-1) and the solvent content is 48.38%. Attempts to solve the structure of mANO1-CTD by the MAD method using selenomethionine-labelled mANO1-CTD or heavy-atom-derivatized crystals are in progress. | - |
dc.format.extent | 3 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.title | Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1 | - |
dc.type | Article | - |
dc.identifier.doi | 10.1107/S1744309111027989 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.67, no.10, pp 1250 - 1252 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000296785700024 | - |
dc.identifier.scopusid | 2-s2.0-80955155451 | - |
dc.citation.endPage | 1252 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1250 | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS | - |
dc.citation.volume | 67 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordAuthor | anoctamin 1 | - |
dc.subject.keywordAuthor | chloride channels | - |
dc.subject.keywordAuthor | transmembrane protein 16A | - |
dc.subject.keywordPlus | ACINAR-CELLS | - |
dc.subject.keywordPlus | CHANNEL | - |
dc.subject.keywordPlus | TMEM16A | - |
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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