Bacterial Luciferase: Determination of the Structure by X-Ray Diffraction
Abstract
This project was focused on determination of the three-dimensional structure of bacterial luciferase. The structure of the enzyme is of fundamental importance to the understanding of the catalytic mechanism and the mode of interaction of the enzyme with accessory proteins, and is essential to future plans to develop biosensor technologies. In the course of this project, numerous crystallization trials were carried out and conditions were refined that permitted high resolution data to be collected and interpreted. In collaboration with Dr. Ivan Rayment of the University of Wisconsin, data have been collected from native crystals and 3 derivatives at 2.8 A. Higher resolution data are being collected at this time, and we fully expect to have a high resolution structure within the next few months, certainly by the end of the calendar year 1994. We have also developed crystallization protocols for several mutant luciferases. Structural analysis of the mutant luciferases should enable us to locate the active site in the three-dimensional structure of the wild-type enzyme, permit mechanistic interpretation of numerous experiments that have been reported over the past ca. 25 years, and assist us in designing the next generation of mutant enzymes to test hypotheses regarding the mechanism of light production by this intriguing and important enzyme.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 20, 1994
- Accession Number
- ADA279699
Entities
People
- Miriam M. Ziegler
- Thomas O. Baldwin
Organizations
- Texas A&M University