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Anaerobic crystallization and initial X‐ray diffraction data of biphenyl 2,3‐dioxygenase from Burkholderia xenovorans LB400: addition of agarose improved the quality of the crystals

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Biphenyl 2,3‐dioxygenase (BPDO; EC catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls (PCBs). BPDOLB400, the terminal dioxygenase component from Burkholderia xenovorans LB400, a proteobacterial species that degrades a broad range of PCBs, has been crystallized under anaerobic conditions by sitting‐drop vapour diffusion. Initial crystals obtained using various polyethylene glycols as precipitating agents diffracted to very low resolution (∼8 Å) and the recorded reflections were diffuse and poorly shaped. The quality of the crystals was significantly improved by the addition of 0.2% agarose to the crystallization cocktail. In the presence of agarose, wild‐type BPDOLB400 crystals that diffracted to 2.4 Å resolution grew in space group P1. Crystals of the BPDOP4 and BPDORR41 variants of BPDOLB400 grew in space group P21.
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Keywords: Burkholderia xenovorans LB400; agarose gel; biphenyl 2,3‐dioxygenase

Document Type: Research Article

Publication date: January 1, 2011

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