Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae
V-ATPases are very complex multi-subunit enzymes which function as proton-pumping rotary nanomotors. The rotary and coupling subunit F (F1-94) was crystallized by the hanging-drop vapour-diffusion method. The native crystals diffracted to a resolution of 2.64 Å and belonged to space group C2221, wit...
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| Format: | Journal Article |
| Language: | English |
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2013
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| Online Access: | https://hdl.handle.net/10356/95360 http://hdl.handle.net/10220/9180 |
| _version_ | 1811690246707871744 |
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| author | Basak, Sandip Balakrishna, Asha Manikkoth Manimekalai, Malathy Sony Subramanian Grüber, Gerhard |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Basak, Sandip Balakrishna, Asha Manikkoth Manimekalai, Malathy Sony Subramanian Grüber, Gerhard |
| author_sort | Basak, Sandip |
| collection | NTU |
| description | V-ATPases are very complex multi-subunit enzymes which function as proton-pumping rotary nanomotors. The rotary and coupling subunit F (F1-94) was crystallized by the hanging-drop vapour-diffusion method. The native crystals diffracted to a resolution of 2.64 Å and belonged to space group C2221, with unit-cell parameters a = 47.21, b = 160.26, c = 102.49 Å. The selenomethionyl form of the F1-94 I69M mutant diffracted to a resolution of 2.3 Å and belonged to space group C2221, with unit-cell parameters a = 47.22, b = 160.83, c = 102.74 Å. Initial phasing and model building suggested the presence of four molecules in the asymmetric unit. |
| first_indexed | 2024-10-01T06:00:57Z |
| format | Journal Article |
| id | ntu-10356/95360 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:00:57Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/953602023-02-28T17:01:56Z Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae Basak, Sandip Balakrishna, Asha Manikkoth Manimekalai, Malathy Sony Subramanian Grüber, Gerhard School of Biological Sciences DRNTU::Science::Chemistry::Biochemistry DRNTU::Science::Chemistry::Crystallography V-ATPases are very complex multi-subunit enzymes which function as proton-pumping rotary nanomotors. The rotary and coupling subunit F (F1-94) was crystallized by the hanging-drop vapour-diffusion method. The native crystals diffracted to a resolution of 2.64 Å and belonged to space group C2221, with unit-cell parameters a = 47.21, b = 160.26, c = 102.49 Å. The selenomethionyl form of the F1-94 I69M mutant diffracted to a resolution of 2.3 Å and belonged to space group C2221, with unit-cell parameters a = 47.22, b = 160.83, c = 102.74 Å. Initial phasing and model building suggested the presence of four molecules in the asymmetric unit. Published version 2013-02-20T02:53:12Z 2019-12-06T19:13:24Z 2013-02-20T02:53:12Z 2019-12-06T19:13:24Z 2012 2012 Journal Article Basak, S., Balakrishna, A. M., Manimekalai, M. S. S., & Grüber, G. (2012). Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(9), 1055-1059. 1744-3091 https://hdl.handle.net/10356/95360 http://hdl.handle.net/10220/9180 10.1107/S1744309112032526 22949193 en Acta crystallographica section F structural biology and crystallization communications © 2012 International Union of Crystallography. This paper was published in Acta Crystallographica Section F Structural Biology and Crystallization Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S1744309112032526]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. application/pdf |
| spellingShingle | DRNTU::Science::Chemistry::Biochemistry DRNTU::Science::Chemistry::Crystallography Basak, Sandip Balakrishna, Asha Manikkoth Manimekalai, Malathy Sony Subramanian Grüber, Gerhard Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae |
| title | Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae |
| title_full | Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae |
| title_fullStr | Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae |
| title_full_unstemmed | Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae |
| title_short | Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V1VO-ATPase from Saccharomyces cerevisiae |
| title_sort | crystallization and preliminary x ray crystallographic analysis of subunit f f1 94 an essential coupling subunit of the eukaryotic v1vo atpase from saccharomyces cerevisiae |
| topic | DRNTU::Science::Chemistry::Biochemistry DRNTU::Science::Chemistry::Crystallography |
| url | https://hdl.handle.net/10356/95360 http://hdl.handle.net/10220/9180 |
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