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Updated: Aug 29, 2026
Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Expression, purification, crystallization and preliminary crystallographic analysis of a putative GTP-binding
Sanjan K Das1, Svetlana E Sedelnikova, Patrick J Baker
1The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
Abstract:
Bacillus subtilis YsxC has been putatively identified as a member of the GTP-binding protein family. Gene-knockout/deletion analysis has suggested that this protein is essential for survival of the microorganism and hence may represent a target for the development of a novel anti-infective agent. The B. subtilis ysxC gene was cloned and the protein was overexpressed in Escherichia coli and subsequently purified. Using hanging-drop vapour-diffusion crystallization techniques, two different crystal forms of YsxC were obtained in the presence and absence of GDP and which have one and two copies of YsxC in the asymmetric unit, respectively. Both crystal forms diffract to beyond 2.0 A resolution and are suitable for structure determination.
