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Updated: Aug 11, 2026

ABCG5/G8 Crystallization in a Lipidic Bicelle Environment for X-Ray Crystallography
Published on: August 25, 2023
Preparation, crystallization and preliminary X-ray analysis of YjcG protein from Bacillus subtilis
Dan Li1, Chiomui Chan, Yu He Liang
1National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871, People's Republic of China.
Abstract:
Bacillus subtilis YjcG is a functionally uncharacterized protein with 171 residues that has no structural homologue in the Protein Data Bank. However, it shows sequence homology to bacterial and archaeal 2'-5' RNA ligases. In order to identify its exact function via structural studies, the yjcG gene was amplified from B. subtilis genomic DNA and cloned into the expression vector pET21-DEST. The protein was expressed in a soluble form in Escherichia coli and was purified to homogeneity. Crystals suitable for X-ray analysis were obtained that diffracted to 2.3 A and belonged to space group C2, with unit-cell parameters a = 99.66, b = 73.93, c = 61.77 A, beta = 113.56 degrees.

