Jim Pitts - Personal Page

Hi there!

I am a senior lecturer here at the Birkbeck Department of Biological Sciences [formally Crystallography]. I started out as a biochemist, then I took my PhD in protein crystallography, followed by more structural molecular biology here at Birkbeck, involving more protein crystallography and homology modelling. I then set-up a recombinant DNA facility to undertake protein engineering using site-directed mutagenesis and expression in micro-organisms. We have targeted the enzyme chymosin and the polypeptide hormone insulin-like growth factor for modification. I teach mainly on recombinant DNA technology and protein structure.

Contact Numbers:              
  e-mail: j.pitts@mail.cryst.bbk.ac.uk
                   Snail-Mail: Department of Biological Sciences,
                   Birkbeck College, University of London,
                   Malet Street, London, WC1E 7HX, UK.


Departmental Safety Adviser,
Departmental Radiation Protection Supervisor,
Departmental Ethics Officer,
Departmental Pastoral Care Tutor,
Departmental Disability Liaison Officer,
  Departmental Library Representative,
Course Director for PPS,
                   College Genetic Modification Safety Adviser,
                   College Laser Safety Officer,
                   First Aider.
College Committee
Chair of the College Programmes Committee,
Chair of the College Post Graduate Science and Social Sciences Board of Examiners,
Teaching and Quality Enhancement Committee (TQEC),
                   Library Policy Committee,
                   College Safety Committee,
Genetic Modification Safety Sub-Committee.

Societies:-        Biochemical Society,
                   British Biophysics Society,
                   British Crystallographic Association,
                   Fellow of the Royal Society of Chemistry,
                   The Higher Education Academy.


1. Engineering Rubisco to change its catalytic properties, Bainbridge, G.M., Madgwick, P., Parmar, S., Keys, A.J., Pitts, J.E. and Parry, M.A.J. (1995) J. Exp. Bot. 46, 1269-1276.

2. The three dimensional X-ray crystal structure of the aspartic proteinase to Trichoderma reesei complexed with a renin inhibitor CP-80794, Pitts, J.E., Crawford, M.D., Nugent, P.G., Wester, R.T., Cooper, J.B., Mantyla, A., Fagerstrom, R. and Nevalainen, H. (1995)  Adv. Exp. Med. Biol. 362, 5437-5446.

3. Solution structure of a mini IGF-1, De Wolf, E., Gill, R., Geddes, S., Pitts, J.E., Wollmer, A. and Grotzinger, J. (1996) Protein Science 5, No.11, 2193-2202.

4. Engineering the C-region of human insulin-like growth factor-1: Implications for receptor binding, Gill, R., Wallach, B., Verma, C., Urso, B., De Wolf, E., Grotzinger, J., Murray-Rust, J., Pitts, J.E., Wollmer, A., De Meyts, P. and Wood, S.P. (1996) Protein Engineering 9, No.11, 1011-1019.

5. Protein engineering loops in aspartic proteinases: Site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin, Nugent, P.G., Albert, A., Orprayoon, P., Wilsher, J., Pitts, J.E., Blundell, T.L. and Dhanaraj, V. (1996) Protein Engineering 9, No.10, 885-893.

6. Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosin, Williams, M.G., Wilsher, J., Nugent, P., Mills, A., Dhanaraj, V., Fabry, M., Sedlacek, J., Uusitalo, J.M., Penttila, M.E., Pitts, J.E. and Blundell, T.L. (1997) Protein Engineering 10, No.9, 991-997.

7. A 2.3 angstrom resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure, Groves, M.R., Dhanaraj, V., Badasso, M., Nugent, P., Pitts, J.E., Hoover, D.J. and Blundell, T.L. (1998) Protein Engineering 11, No.10, 833-840.

8. Effect of mutation of lysine-128 of the large subunit of ribulose bisphosphate carboxylase/oxygenase from Anacystis nidulans, Bainbridge, G., Anralojc, P.J., Madgwick, P.J., Pitts, J.E. and Parry, M.A.J. (1998) Biochemical Journal 336, No. Pt. 2, 387-393.

9. Protein engineering aspartic proteinases - Site-directed mutagenesis, biochemical characterization, and X-ray analysis of chymosins with substituted single amino acid substitutions and loop replacements, Albert, A., Blundell, T.L., Dhanaraj, V., Donate, L.E., Groves, M., Guruprasad, K., Nugent, P.G., Orprayoon, P., Pitts, J.E., Rufino, S., Srinivasan, N., Williams, M. and Wilsher, J. (1998) Advances in Experimental Medicine and Biology 436, 169-177.

10. Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: implications for receptor binding, Gill, R., Verma, C., Wallach, B., Ursų, B., Pitts, J.E., Wollmer, A., De Meyts, P. and Wood, S.P. (1999) Protein Engineering 12, No.4, 297-303.

11. Crystallization of Helix pomatia agglutinin (HPA), a protein from the edible snail, Lisgarten, J.N., Pitts, J.E., Palmer, R.A., Reynolds, C.D., Dao-Thi, M.H., Van Driessche, E. and Beeckmans, S. (1999) Acta Cryst. D55, 1903-1905.

12. Structure-function studies of an IGF-I analogue that can be chemically cleaved to a two-chain mini-IGF-I, Geddes, S., Holst, P., Grotzinger, J., Gill, R., Nugent, P., De Meyts, P., Wollmer, A., Wood, S.P. and Pitts, J.E. (2001) Protein Engineering 14, No.1, 61-65.

13. Structure and function of human insulin-like growth factor-1, Gill, R., De Meyts, P., Pitts, J.E., Verma, C., Wollmer, A. and Wood, S.P. (2002) Recent Res. Devel. Protein Eng. 2, 105-134 [ISBN: 81-7736-147-3].