Related Experiment Video
Updated: Aug 10, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Protein expression, crystallization and preliminary X-ray crystallographic studies of YjbK from Bacillus subtilis
Xue-Yu Dai1, Yuan Liu, Yu-He Liang
1National Laboratory of Protein Engineering and Plant Genetic Engineering, China.
Abstract:
B. subtilis YjbK is a protein with 190 residues of uncharacterized function, it has been annotated by Pfam database as a member of adenylate cyclase family (EC: 4.6.1.1). In order to identify its exact function via structural studies, yjbK gene was amplified from B. subtilis genomic DNA and cloned into expression vector pET21-DEST. The protein was expressed in a soluble form in E. coli and purified to homogeneity. YjbK was crystallized and diffracted to a resolution of 2.0 A in-house. The crystals belong to P1 space group, with unit cell parameters a = 32.38 A, b = 34.69 A, c = 46.02 A, alpha = 96.560 degrees, beta = 99.683 degrees, gamma = 111.333 degrees. There is one molecule per asymmetric unit.

