Related Experiment Video
Updated: May 12, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
1.37 Å crystal structure of pathogenic factor pectate lyase from Acidovorax citrulli
Qun Tang1, Yan-Ping Liu, Zheng-Guang Ren
1Department of Plant Pathology, China Agricultural University, Beijing, China.
Abstract:
Pectates lyase (Pel) plays an important role in bacteria pathogenicity. The crystal structure of Pel from Acidovorax citrulli (AcPel) has been solved to 1.37 Å resolution. AcPel belongs to the polysaccharide lyase family 1 (PL1), which has a characteristic right-handed β-helix fold. AcPel is similar with other Pels in the PL1 family, but also shows some differences at the substrate binding site.
More Related Videos
10:21Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020