Contact info:
Lawrence Berkeley National Laboratory
One Cyclotron Road
Mail Stop: 234 Calvin Lab
Berkeley, California 94720
USA

Location: 3-250
Phone: (510) 486-4335
Fax: (530) 323-9836
Email: EABerry@lbl.gov

Web site 1: The Ed Berry Research Group

Web site 2: Cytochrome bc1 project

Research emphasis
My main interest is in the mechanism and apparatus of biological energy transducing processes, and especially the respiratory and photosynthetic electron transfer chains that convert redox energy (from foodstuffs or from light-driven reactions) into a transmembrane gradient in the electrochemical potential of the hydrogen ion (proton).

The reactions of the electron transfer chains are catalyzed by large, transmembrane protein complexes, and so studying these processes has necessitated learning techniques for extracting and purifying these membrane protein complexes. One of the major roadblocks to understanding these processes has been the lack of atomic-resolution structural information about the enzymes involved, so for the last 10 years my group has been working mainly on extending our purification expertise to crystallization and structure determination of the proteins involved. We are carrying out this effort as a part of the Structural Biology Department under the auspices of Sung-Hou Kim. In early 1998 my group in collaboration with the Kim group published the structure of the cytochrome bc1 complex, the central component of the mitochondrial respiratory chain. This was the first structure of this complex to include all three of the redox-active protein components. We have continued to develop new improved crystal forms of this complex, and today we are refining a high resolution (2 A) structure that includes vastly more detailed information than the early low-resolution structures. Recently we solved the structure of the related bacterial cytochrome bc1 complex (Rb. capsulatus) but at lower resolution; current efforts are directed at improving these crystals.

We have also determined the only structure available for the mitochondrial Complex II protein, and are working on improving the crystals and the structure. Other related proteins we have crystallized and/or solved include cytochrome oxidase, cytochrome f, cytochrome c2, and chicken mitochondrial cytochrome c. We are preparing to apply the expertise gained through these efforts to obtaining a structure for the chloroplast cytochrome b6f/FNR complex, the remaining unsolved component of the chloroplast photosynthetic electron transfer chain.

Publications