WELCOME TO THE GARAVITO LAB PAGE

RESEARCH FOCI

The focus of the laboratory is on the determination of the 3-dimensional structures of biological macromolecules by X-ray crystallography and the elucidation of their structure-function relationships. Of major interest are the structures of integral membrane proteins, enzymes involved in the biosynthesis of membrane components, and large macromolecular complexes that interact with biological membranes.

LAB PERSONNEL

R. Michael Garavito - Professor, aka "El Jefe" garavito@msu.edu

Rachel Powers - Research Associate

Nicole Webb - Graduate Student

Christine Harman - Graduate Student (with Bill Smith)

Yi Zheng - Graduate Student

Yanfeng Zhang - Graduate Student

Young-Cho Moon - Graduate Student

Amy Scharmen - Research Technical Assistant

Dexin Sui - Research Technical Assistant

Past and Long-term Projects

Some of the former projects which we have worked on include small peptide structures and E. coli outer membrane porins .  However, we also have had a long-term research effort to develop methods for crystallizing membrane proteins.  Some of results and discussions can be found in:

Garavito, R. M. and Picot, D. (1990)  Methods: A Companion to Methods in Enzymology 1, 57-69.
Garavito, R. M. and Picot, D. (1991)   J. Crystal Growth 110, 89-95.
Garavito, R. M., Picot, D., and Loll, P. J. (1996)  J. Bioenergetics and Biomembranes 28, 13-27.
Garavito, R. M., and Ferguson-Miller, S. (2001)  J. Biol. Chem.276, 32403-6.

CURRENT PROJECTS


A view of the PGHS-1 dimer. Work on the structure/function relationships PGHS isoforms 1 and 2 with regards to the cyclooxygenase reaction is a major focus of the laboratory.


A view of the PGHS peroxidase active site. Efforts are underway to explore the nature of the PGHS peroxidase reaction.

 


The structure/function relationships in mammalian hexokinases , particularly with regard to membrane interactions is another focus of the laboratory.


The reaction mechanisms for the biosynthesis of novel sugar-nucleotides by the SDR family of enzymes like SQD1 (above) is another focus of the laboratory.

 


The structure/function relationships in family 1 glycosyltransferases particularly with regard to antibiotic biosynthesis and membrane biogenesis are actively being studied.


The reaction mechanisms of cytochrome c oxidase is being studied by mutagenesis (Ferguson-Miller laboratory) and by X-ray crystallography (Garavito laboratory).

 

513 Biochemistry Building
Michigan State University
East Lansing, MI
(517) 353-9125

OTHER LINKS AT MSU

Department of Biochemistry Macromolecular Computing Facility
Structure and Computational Biology Group
Biomacromolecular Crystallography


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