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Updated: May 13, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Purification, crystallization and preliminary crystallographic analysis of the marine α-amylase AmyP
Jigang Yu1, Chengliang Wang, Yanjin Hu
1School of Life Sciences, Anhui University, Hefei, Anhui 230039, People's Republic of China.
Abstract:
AmyP is a raw-starch-degrading α-amylase newly identified from a marine metagenome library. It shares low sequence similarity with characterized glycoside hydrolases and was classified into a new subfamily of GH13. In particular, it showed preferential degradation to raw rice starch. Full-length AmyP was cloned and overexpressed in Escherichia coli, then purified and crystallized in the presence of its substrate analogue β-cyclodextrin. X-ray diffraction data were collected to a resolution of 2.1 Å. The crystal belonged to space group P2₁2₁2, with unit-cell parameters a=129.824, b=215.534, c=79.699 Å, α=β=γ=90°, and was estimated to contain two molecules in one asymmetric unit.

