May, 2006
Crystallization and preliminary X-ray analysis of an exotype alginate lyase Atu3025 from Agrobacterium tumefaciens strain C58, a member of polysaccharide lyase family 15
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
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- Volume
- 62
- Number
- Pt 5
- First page
- 486
- Last page
- 488
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1107/S1744309106014333
- Publisher
- INT UNION CRYSTALLOGRAPHY
Almost all alginate lyases depolymerize alginate in an endolytical fashion via a beta-elimination reaction. The alginate lyase Atu3025 from Agrobacterium tumefaciens strain C58, consisting of 776 amino-acid residues, is a novel exotype alginate lyase classified into polysaccharide lyase family 15. The enzyme was crystallized at 293 K by sitting-drop vapour diffusion with polyethylene glycol 4000 as a precipitant. Preliminary X-ray analysis showed that the Atu3025 crystal belonged to space group P2(1) and diffracted to 2.8 angstrom resolution, with unitcell parameters a = 107.7, b = 108.3, c = 149.5 angstrom, beta = 91.5 degrees.
- Link information
- ID information
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- DOI : 10.1107/S1744309106014333
- ISSN : 2053-230X
- Web of Science ID : WOS:000237159000018