Skip to main content
padlock icon - secure page this page is secure

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

Buy Article:

$52.00 + tax (Refund Policy)

Biphenyl 2,3‐dioxygenase (BPDO; EC 1.14.12.18) 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.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Burkholderia xenovorans LB400; agarose gel; biphenyl 2,3‐dioxygenase

Document Type: Research Article

Publication date: January 1, 2011

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more