Research
James uses a wide range of molecular biology and biochemical techniques for the cloning, expression and purification of proteins and nucleic acids for analysis by biophysical techniques such as EMSAs, light scattering (dynamic and multi-angle laser), analytical ultra-centrifugation (sedimentation equilibrium and sedimentation velocity) and structural studies utilising circular diochroism, NMR, small-angle X-ray and small-angle neutron scattering.
James initially worked on Type I bacterial Restriction-Modification (R-M) systems; complex multi-subunit complexes involved in methylation and cleavage of DNA. He investigated the structure, activity, subunit interactions and DNA-induced conformational changes of the methyltransferase and restriction endonuclease complexes. He developed small-angle neutron scattering techniques, utilising selective deuteration with contrast variation to enable the location of each subunit in situ. This work, including the low resolution structure of a Type I DNA methyltransferase, was featured on the front cover of JMB and in the 2010 ILL Annual Report.
More recently, James has helped solve the solution structure of Type I DNA restriction endonuclease, circa 402 kDa, which has recently been accepted for publication by the journal Genes and Development.
James has also worked on the structure and function of the calmodulin (HIV-1) matrix complex (CaM-MA); the anti-toxin/toxin complex, VapBC; cryoglobulins and cardiac binding myosin protein C (cMyBP-C). Currently, James is helping to solve the solution structures of E.coli and Vibriocholera Hfq in complex with a number of RNA substrates. More broadly, James is interested in protein-protein and protein-nucleic interactions in complex multi-subunit systems.