Published April 28, 2006 | Version v1
Journal article

Crystallization and preliminary X-ray analysis of an exotype alginate lyase Atu3025 from Agrobacterium tumefaciens strain C58, a member of polysaccharide lyase family 15

  • 1. Laboratory of Basic and Applied Molecular Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011 (Japan)
  • 2. Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011 (Japan)

Description

The crystallization and preliminary X-ray characterization of a family PL-15 exotype alginate lyase are presented. Almost all alginate lyases depolymerize alginate in an endolytical fashion via a β-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 P21 and diffracted to 2.8 Å resolution, with unit-cell parameters a = 107.7, b = 108.3, c = 149.5 Å, β = 91.5°

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309106014333; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2219967

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
62
Journal Issue
Pt 5
Journal Page Range
p. 486-488
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46061485
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTALLIZATION; CRYSTALS; DIFFUSION; RESOLUTION; SPACE GROUPS; STRAINS
Descriptors DEC
PHASE TRANSFORMATIONS; SYMMETRY GROUPS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2006
Notes
PMCID: PMC2219967; PMID: 16682783; PUBLISHER-ID: bw5139; OAI: oai:pubmedcentral.nih.gov:2219967