The University of Sheffield
Department of Molecular Biology and Biotechnology

Structural Studies


Dr G C Ford
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In this laboratory, the research and teaching are concerned with the use of X-ray crystallography in the determination of the structures of macromolecules and with the application of computation in that field.

 

Some crystallographic investigations underway address the determination of the spatial structures of redox proteins with an FMN prosthetic group, Flavodoxin B from Azotobacter chrococcum, and a haem prosthetic group, cytochrome b-562 from Erwinia chrysanthemi.

 

On the computation front, development continues for PepSig - yet another program to use the ribbon paradigm of Jane Richardson as coded by John Priestle - as a vehicle for the pleasing display of the structures of proteins.

 

In addition, the application of IT to act as a teaching resource has generated a number of Computer Tutorials in aspects of Molecular Biology.
Schematic graphic of the FMN dependent protein Schematic graphic of the FMN dependent protein Figure legend. Schematic graphic of the FMN dependent protein ec from the di-nitrogen fixing bacterium Azotobacter chrococcum. The graphic was generated in program PepSig.

 

Selected Publications

Structure of lactate dehydrogenase at 2.8A resolution. Adams, M.J., Ford, G.C., Keokoek, R., Lentz, P.J. Jnr., McPherson, A. Jnr., Rossmann, M.G., Smiley, I.E., Schevitz, R.W., Wonacott, A.J. (1970), Nature (London) 227, 1098-1103.
D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance. Buehner, M., Ford, G.C., Moras, D., Olsen, K.W., Rossmann, M.G., (1973) Proc.Nat.Acad.Sci. U.S.A. 70, 3052-3054.
A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes. White, J.L., Hackert, M.L., Buehner, M., Adams, M.J., Ford, G.C., Lentz, P.J.Jnr., Smiley, I.E., Steindel, S.J., Rossmann, M.G. (1976). J. Molec. Biol. 102, 759-779.
Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate amino-transferase. Ford, G.C., Eichele, G., Jansonius, J.N. (1980). Proc.Natl.Acad.Sci. U.S.A. 77, 2559-2563.
Ferritin: design and formation of an iron-storage molecule. Ford, G.C., Harrison, P.M., Rice, D.W., Smith, J.M.A., Treffry, A., White, J.L. and Yariv, J. (1984). Philosophical Transactions of the Royal Society London, B.304, 551-565
Mechanisms of action of aspartate aminotransferase proposed on the basis of its spatial structure. Kirsch, J.F., Eichele, G., Ford, G.C., Vincent, M.G., Jansonius, J.N., Gehring, H. and Christen, P. (1984) Journal of Molecular Biology, 174, 497-525.
Restrained least-squares refinement of the sulphydryl Protease Papain to 2.0A. Priestle, J., Ford, G.C., Glor, M., Mehler, E.L., Smit, J.D.G., Thaller, C., Jansonius, J.N. (1984). Acta Crystallographica A40, C17.
Pep-Sig : the manual. (1988 - date)
Selection of a thermostable variant of chloramphenicol acetyltransferase (Cat-86). Turner,S.L., Ford, G.C., Mountain, A., & Moir, A. (1992) Protein Engineering 5(6): 535-541
Flavodoxins and Nitrogen fixation -Structure, Electrochemistry and Post-translational Modification by Coenzyme A. R.N.F.Thorneley, G.A.Ashby, M.H.Drummond, R.R.Eady, D.L.Hughes, G.C.Ford, P.M.Harrison, A.Shaw, R.L.Robson, J.Kazaluskaite & H.A.O. Hill. (1993) in : Flavins & Flavoproteins, de Gruyter, Berlin.
Crystallization of cytochrome B-562 from Erwinia chrysanthemi. Wilkinson, K.W, Ford, G.C, Moir, A.J, Rice, D.W, Rodgers, H.F, Smith, J.M.A, Stillman, T.J, & Goward.C.R (1997) Acta Crystallographica Section D Biological Crystallography 53(2): 197-199
Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. Hempstead, P.D, Yewdell, S.J, Fernie, A.R, Lawson, D.M, Artymiuk, P.J, Rice, D.W, Ford, G.C, & Harrison.P.M (1997) J Molec Biol 268(2): 424-448