Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium
Recombinant citrate synthase from a psychrotolerant bacterium, DS2-3R, recently isolated in Antarctica, has been crystallized. The crystals belong to space group P6(1)22 or P6(5)22, with cell dimensions a = b = 70.8, c = 307.8 Angstrom. Diffraction data collected on a synchrotron from a cryoprotecte...
| Main Authors: | , , , , , |
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| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
1998
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| Subjects: | |
| Online Access: | https://research-portal.st-andrews.ac.uk/en/publications/992acf5f-1fdc-43fd-b77a-d71c16ea6283 http://www.scopus.com/inward/record.url?scp=0032168527&partnerID=8YFLogxK |
| _version_ | 1824227506195005440 |
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| author | Gerike, U Russell, RJM Danson, MJ Russell, N Hough, DW Taylor, Garry Lindsay |
| author_facet | Gerike, U Russell, RJM Danson, MJ Russell, N Hough, DW Taylor, Garry Lindsay |
| author_sort | Gerike, U |
| collection | University of St Andrews: Research Portal |
| description | Recombinant citrate synthase from a psychrotolerant bacterium, DS2-3R, recently isolated in Antarctica, has been crystallized. The crystals belong to space group P6(1)22 or P6(5)22, with cell dimensions a = b = 70.8, c = 307.8 Angstrom. Diffraction data collected on a synchrotron from a cryoprotected crystal extend to at least 2.0 Angstrom. Knowledge of the structure of this enzyme Rill add to the understanding of told activity and thermolability and will be of biotechnological interest. Previously, the structure of citrate synthase from Archaea inhabiting environments at 328 and 373 K, has been reported. This present study will extend our understanding of the structural integrity and activity of proteins at the temperature extremes of life. |
| format | Article in Journal/Newspaper |
| genre | Antarc* Antarctic Antarctica |
| genre_facet | Antarc* Antarctic Antarctica |
| geographic | Antarctic |
| geographic_facet | Antarctic |
| id | ftunstandrewcris:oai:research-portal.st-andrews.ac.uk:publications/992acf5f-1fdc-43fd-b77a-d71c16ea6283 |
| institution | Open Polar |
| language | English |
| op_collection_id | ftunstandrewcris |
| op_rights | info:eu-repo/semantics/restrictedAccess |
| op_source | Gerike , U , Russell , RJM , Danson , MJ , Russell , N , Hough , DW & Taylor , G L 1998 , ' Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium ' , Acta Crystallographica. Section D, Biological crystallography , vol. 54 , pp. 1012-1013 . |
| publishDate | 1998 |
| record_format | openpolar |
| spelling | ftunstandrewcris:oai:research-portal.st-andrews.ac.uk:publications/992acf5f-1fdc-43fd-b77a-d71c16ea6283 2025-02-16T14:59:40+00:00 Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium Gerike, U Russell, RJM Danson, MJ Russell, N Hough, DW Taylor, Garry Lindsay 1998-09-01 https://research-portal.st-andrews.ac.uk/en/publications/992acf5f-1fdc-43fd-b77a-d71c16ea6283 http://www.scopus.com/inward/record.url?scp=0032168527&partnerID=8YFLogxK eng eng info:eu-repo/semantics/restrictedAccess Gerike , U , Russell , RJM , Danson , MJ , Russell , N , Hough , DW & Taylor , G L 1998 , ' Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium ' , Acta Crystallographica. Section D, Biological crystallography , vol. 54 , pp. 1012-1013 . CRYSTAL-STRUCTURE PYROCOCCUS-FURIOSUS RESOLUTION CRYSTALLIZATION PROTEINS ARCHAEON article 1998 ftunstandrewcris 2025-01-24T05:31:15Z Recombinant citrate synthase from a psychrotolerant bacterium, DS2-3R, recently isolated in Antarctica, has been crystallized. The crystals belong to space group P6(1)22 or P6(5)22, with cell dimensions a = b = 70.8, c = 307.8 Angstrom. Diffraction data collected on a synchrotron from a cryoprotected crystal extend to at least 2.0 Angstrom. Knowledge of the structure of this enzyme Rill add to the understanding of told activity and thermolability and will be of biotechnological interest. Previously, the structure of citrate synthase from Archaea inhabiting environments at 328 and 373 K, has been reported. This present study will extend our understanding of the structural integrity and activity of proteins at the temperature extremes of life. Article in Journal/Newspaper Antarc* Antarctic Antarctica University of St Andrews: Research Portal Antarctic |
| spellingShingle | CRYSTAL-STRUCTURE PYROCOCCUS-FURIOSUS RESOLUTION CRYSTALLIZATION PROTEINS ARCHAEON Gerike, U Russell, RJM Danson, MJ Russell, N Hough, DW Taylor, Garry Lindsay Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium |
| title | Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium |
| title_full | Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium |
| title_fullStr | Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium |
| title_full_unstemmed | Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium |
| title_short | Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium |
| title_sort | preliminary crystallographic studies of citrate synthase from an antarctic psychrotolerant bacterium |
| topic | CRYSTAL-STRUCTURE PYROCOCCUS-FURIOSUS RESOLUTION CRYSTALLIZATION PROTEINS ARCHAEON |
| topic_facet | CRYSTAL-STRUCTURE PYROCOCCUS-FURIOSUS RESOLUTION CRYSTALLIZATION PROTEINS ARCHAEON |
| url | https://research-portal.st-andrews.ac.uk/en/publications/992acf5f-1fdc-43fd-b77a-d71c16ea6283 http://www.scopus.com/inward/record.url?scp=0032168527&partnerID=8YFLogxK |