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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 438–442.
Published online Apr 20, 2007. doi:  10.1107/S1744309107018787
PMCID: PMC2335002
The crystallization of apo-form UMP kinase from Xanthomonas campestris is significantly improved in a strong magnetic field
Jhe-Le Tu,a Ko-Hsin Chin,ab Andrew H.-J. Wang,cd and Shan-Ho Chouab*
aInstitute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan
bNational Chung-Hsing University Biotechnology Center, National Chung-Hsing University, Taichung 40227, Taiwan
cInstitute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan
dCore Facility for Protein Crystallography, Academia Sinica, Nankang, Taipei, Taiwan
Correspondence e-mail: shchou/at/nchu.edu.tw
Received March 16, 2007; Accepted April 16, 2007.
Abstract
Bacterial UMP kinases (UMPKs) are crucial enzymes that are responsible for microbial UTP biosynthesis. Interestingly, eukaryotic and prokaryotic cells use different enzymes for UMP-phosphorylation reactions. Prokaryotic UMPKs are thus believed to be potential targets for antimicrobial drug development. Here, the cloning, expression and crystallization of SeMet-substituted XC1936, a bacterial UMPK from Xanthomonas campestris pathovar campestris, are reported. The crystallization of the apo-form UMPK was found to be significantly improved in a strong magnetic field; the crystals diffracted to a resolution of 2.35 Å, a dramatic improvement over the original value of 3.6 Å. Preliminary structural analyses of apo-form XC1936 using crystals grown in a strong magnetic field clearly reveal well defined loop regions involved in substrate-analogue binding that were previously not visible. Crystallization in a strong magnetic field thus was found to be indispensable in determining the flexible region of the XC1936 UMPK structure.
Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of
International Union of Crystallography