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Updated: Jun 3, 2026
Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus
Ahmed Akrem1, Sadaf Iqbal, Friedrich Buck
1Department of Chemistry, University of Hamburg, c/o DESY, Laboratory for Structural Biology of Infection and Inflammation, Notkestrasse 85, 22603 Hamburg, Germany.
Abstract:
A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30 kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=172.3, b=37.1, c=126.4 Å, β=127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1 Å.
