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Updated: Jan 31, 2026
Improvement of Bacillus subtilis Spore Enumeration and Label Analysis in Flow Cytometry
Published on: June 30, 2023
Purification, crystallization and preliminary X-ray analysis of a putative nucleotide phosphohydrolase, YpgQ, from
Ye Ji Jeon1, Wan Seok Song1, Sung-il Yoon1
1Department of Systems Immunology, College of Biomedical Science, Kangwon National University, Chuncheon 200-701, Republic of Korea.
Abstract:
The histidine-aspartate (HD) domain exerts phosphohydrolase activity on nucleotides and functions in nucleotide metabolism. Sequence analysis suggested that YpgQ from Bacillus subtilis contains the HD domain, but the structure and function of YpgQ remain to be revealed. The recombinant YpgQ protein was overexpressed in an Escherichia coli cell expression system and was purified to homogeneity by Ni-NTA affinity and anion-exchange chromatography. Crystals in space group P2₁ were obtained in PEG 600 solutions and diffracted X-rays to 2.3 Å resolution. Moreover, X-ray fluorescence scans on YpgQ crystals demonstrated the metal-binding ability of YpgQ.
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