The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions.

@article{Fisher1996The1R,
  title={The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions.},
  author={Andrew J Fisher and Thomas B Thompson and James B. Thoden and Thomas O. Baldwin and Ivan Rayment},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 36},
  pages={21956-68}
}
Bacterial luciferase is a flavin monooxygenase that catalyzes the oxidation of a long-chain aldehyde and releases energy in the form of visible light. A new crystal form of luciferase cloned from Vibrio harveyi has been grown under low-salt concentrations, which diffract x-rays beyond 1.5-A resolution. The x-ray structure of bacterial luciferase has been refined to a conventional R-factor of 18.2% for all recorded synchrotron data between 30.0 and 1.50-A resolution. Bacterial luciferase is an… CONTINUE READING

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