Related Experiment Video
Updated: Aug 10, 2026
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Protein preparation, crystallization and preliminary X-ray crystallographic studies of dihydroorotase from Bacillus
Yu-He Liang1, Xiangyu Liu, Juan Wang
1National Laboratory of Protein Engineering and Plant Genetic Engineering, Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing 100871, China.
Abstract:
B. subtilis dihydroorotase is an important enzyme in de novo pyrimidine biosynthesis pathway and encoded by pyrC gene in pyr operon. pyrC was amplified from B. subtilis genomic DNA and cloned into expression vector pET21-DEST. Dihydroorotase was expressed soluble form in E. coli and purified. The protein was crystallized and diffracted to 2.2 A. The crystal belongs to P2(1)2(1)2(1) space-group, with unit cell parameters a = 48.864 A, b = 84.99 A, c = 203.05 A. There are 2 molecules per asymmetry unit.
More Related Videos
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
12:23Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017