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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Dabin, Jérôme Jam, Murielle Czjzek, Mirjam Michel, Gurvan |
| Description | Country affiliation: France Author Affiliation: Dabin J ( UPMC University Paris 06, UMR 7139, Marine Plants and Biomolecules, Station Biologique de Roscoff, F-29682 Roscoff, Bretagne, France.) |
| Abstract | Polysaccharide lyases belonging to family PL1 act on pectins. These anionic polymers are usually produced by terrestrial plants and therefore pectinolytic enzymes are not frequently observed in marine microorganisms. The protein RB5312 from the marine bacterium Rhodopirellula baltica is distantly related to family PL1 pectate lyases, but its exact function is unclear. In this study, the expression and purification of a recombinant form of RB5312 are described. This protein was crystallized using the hanging-drop vapour-diffusion method. The crystals belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 39.05, b = 144.05, c = 153.97 A, alpha = beta = gamma = 90 degrees. A complete data set was collected to 1.8 A resolution from a native crystal. |
| File Format | HTM / HTML |
| ISSN | 2053230X |
| e-ISSN | 17443091 |
| DOI | 10.1107/S1744309108004387 |
| Journal | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
| Issue Number | Pt 3 |
| Volume Number | 64 |
| Language | English |
| Publisher | Wiley |
| Publisher Date | 2008-03-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Bacteria Enzymology Gene Expression Polysaccharide-lyases Chemistry Isolation & Purification Genetics Cloning, Molecular Crystallization Oceans And Seas Metabolism X-ray Diffraction Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics |
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