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PMID: 2195018 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Preliminary crystallographic analysis of the plant pathogenic factor, pectate lyase C from Erwinia chrysanthemi.

The Journal of biological chemistry ·Vol. 265 ·No. 20 ·1990-07-15 ·Pages 11429-31

Yoder MD, DeChaine DA, Jurnak F

Abstract

Pectate lyases are saccharide-binding enzymes that degrade plant cell walls. One pectate lyase from Erwinia chrysanthemi (EC16), termed pectate lyase C, has been crystallized from ammonium sulfate. The preliminary x-ray diffraction analysis indicates that the crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions, a = 73.4 A, b = 80.3 A, and c = 95.1 A. The crystals diffract to a resolution of 2.2 A and have one molecule/asymmetric unit.

MeSH Terms
Ammonium Sulfate Cloning, Molecular Crystallization Erwinia/enzymology,genetics,pathogenicity Escherichia coli/genetics Plants/microbiology Plasmids Polysaccharide-Lyases/genetics,isolation & purification X-Ray Diffraction
Chemicals
Polysaccharide-Lyases pectate lyase Ammonium Sulfate
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yoder M D
Department of Biochemistry, University of California, Riverside 92521.
DeChaine D A
Jurnak F
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1990-07-15
Pages
11429-31
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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