Papers

Peer-reviewed
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
  • A Ochiai
  • ,
  • M Yamasaki
  • ,
  • B Mikami
  • ,
  • W Hashimoto
  • ,
  • K Murata

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
DOI
https://doi.org/10.1107/S1744309106014333
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000237159000018&DestApp=WOS_CPL
ID information
  • DOI : 10.1107/S1744309106014333
  • ISSN : 2053-230X
  • Web of Science ID : WOS:000237159000018

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