Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris

Journal Article · Fri Jul 01 04:00:00 EDT 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309105018956· OSTI ID:22356136

Chin, Ko-Hsin ^[1]; Chou, Chia-Cheng; Lee, Cheng-Chung; Shr, Hui-Lin ^[2]; Lyu, Ping-Chiang ^[3]; Wang, Andrew H.-J. ^[2]; Chou, Shan-Ho ^[1]

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1. Institute of Biochemistry, National Chung-Hsing University, Taichung 40227,Taiwan (China)
2. Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei,Taiwan (China)
3. Department of Life Science, National Tsing Hua University, Hsin-Chu,Taiwan (China)

A putative ApaG gene product from X. campestris pv. campestris was overexpressed in E. coli, purified and crystallized. The crystals diffracted to a resolution of at least 2.3 Å. Xanthomonas campestris pv. campestris is the causative agent of black rot, one of the major worldwide diseases of cruciferous crops. Its genome encodes approximately 4500 proteins, roughly one third of which have unknown function. XC2382 is one such protein, with a MW of 14.2 kDa. Based on a bioinformatics study, it was annotated as an ApaG gene product that serves multiple functions. The ApaG protein has been overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of at least 2.30 Å. They are tetragonal and belong to space group P4{sub 1/3}, with unit-cell parameters a = b = 57.6, c = 122.9 Å. There are two, three or four molecules in the asymmetric unit.

• OSTI ID: 22356136
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

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