Crystallization and preliminary X-ray crystallographic analysis of the XoGroEL chaperonin from Xanthomonas oryzae pv. oryzae

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 70; no. 5; pp. 604 - 607
• Main Authors: Tran, Huyen-Thi, Pham, Tan-Viet, Ngo, Ho-Phuong-Thuy, Hong, Myoung-Ki, Kim, Jeong-Gu, Lee, Sang Hee, Ahn, Yeh-Jin, Kang, Lin-Woo
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-05-2014; Wiley Subscription Services, Inc
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; chaperone; Chaperonins - chemistry; Chaperonins - isolation & purification; Crystallization; Crystallization Communications; Crystallography, X-Ray; GroEL; Xanthomonas; Xanthomonas oryzae pv. oryzae (Xoo); chaperone; GroEL; Xanthomonas oryzae pv. oryzae (Xoo)
• ISSN: 2053-230X; 2053-230X
• DOI: 10.1107/S2053230X14006591

Along with the co‐chaperonin GroES, the chaperonin GroEL plays an essential role in enhancing protein folding or refolding and in protecting proteins against misfolding and aggregation in the cellular environment. The XoGroEL gene (XOO_4288) from Xanthomonas oryzae pv. oryzae was cloned and the protein was expressed, purified and crystallized. The purified XoGroEL protein was crystallized using the hanging‐drop vapour‐diffusion method and a crystal diffracted to a resolution of 3.4 Å. The crystal belonged to the orthorhombic space group P212121 with 14 monomers in the asymmetric unit, with a corresponding VM of 2.7 Å3 Da−1 and a solvent content of 54.5%.