Structural Biology


In the structural biology theme, X-ray crystallography and NMR are combined as extremely powerful techniques to explore the structure of macromolecules at the highest level of atomic detail. The dynamic behaviour of proteins in solution and how they assemble into their complex folds is explored, with emphasis on protein mis-folding in disease states such as Alzheimer's. High power electron and atomic force microscopy is used to visualise biological assemblies and processes directly, while complementary fluorescence microcopy is used to visualise complex organisation and localisation in vivo. Such large datasets require expertise in computational biology to analyse and interpret results.

Structural biology research in our department at a glance:

  • X-ray protein crystallographyprotein complexes, especially of toxins and virulence factors, protein/DNA interactions, drug design
  • Nuclear magnetic resonance spectroscopy (NMR)protein structure and dynamics, molecular interactions, ligand binding, high-pressure NMR
  • Complex imaging - fluorescence microscopy, electron microscopy (EM), atomic force microscopy (AFM), cryoelectron tomography
  • Computational biology - protein structure modelling, dynamic system modelling, image analysis

For further information and research opportunities, please see the staff page of individual researchers below:


Dr Patrick Baker

Director Of Studies and Deputy Head of Department

Room: D5e/D14a
0114 222 2725

Use of protein crystallography to study the structure/function relationships in biological macromolecules, including substrate specificity and chiral synthesis in enzymes and the molecular basis of stability in proteins from extremophiles.

Julien Bergeron

Dr Julien Bergeron

starts Spring 2017

Structural studies of bacterial nano-machines, in particular the bacterial flagellum, the bacterial cytoskeleton, and the T3SS injectisome. Hybrid methods for structural characterisation, using EM, X-ray, NMR and computer modelling.


Prof Per Bullough

Room: E36e
0114 222 4245

Solving the assembly and structure of large and challenging protein assemblies by high resolution electron microscopy (cryoEM) and X-ray crystallography, in particular bacterial endospores, cell surfaces and membrane protein complexes.


Dr Jeremy Craven

Room: D14b
0114 222 4323

Computational methods to model system dynamics in organisms, including hyphal tip growth in the pathogenic fungus Candida albicans, and peroxisome development in yeast. Image analysis.


Dr Egbert Hoiczyk

Room: F21
0114 222 2733

Using light and electron microscopy to study the structure and function of bacterial ultra-structure. Particular interest in bacterial cytoskeletons, gliding motility complexes and nano-organelles.



Prof Neil Hunter FRS

Krebs Chair in Biochemistry

Room: E14a
0114 222 4191

Biogenesis, structure, function and nanotechnology of photosynthetic membrane proteins from phototrophic bacteria and plants. Enzymology of the chlorophyll and carotenoid biosynthesis pathways.



Dr Ling Chin Hwang

Room: E10
0114 222 2847

Multidisciplinary techniques such as single-molecule imaging, synthetic biology, biochemistry and microfluidics to study the molecular mechanisms of spatial organization in bacteria, such as cell division and chromosome segregation.


Dr Matt Johnson

Room: E6a
0114 222 4418

Structure and function of the higher plant photosynthetic thylakoid membrane using atomic force microscopy and stochastic super-optical microscopy (STORM/ PALM) combined with membrane biochemistry.



Dr John Rafferty

Room: D8a
0114 222 2809

Structural study of proteins and DNA primarily by X-ray crystallography and electron microscopy to gain 3D insights of biological macromolecules and their assemblies. Structure and function relationships.


Prof David Rice

Harrison Chair in Structural Biology

Room: D8c
0114 222 4242

X-ray crystallography in the analysis of enzyme structure and function to develop an understanding of basic biological mechanisms for rational design of new drugs and the use of enzymes for industrial and biomedical applications.


Dr Rosie Staniforth

Room: D7a
0114 222 2761

Structural and mechanistic studies on the mechanism of amyloid fibril formation, the precursor to neurodegenrative conditions including Alzheimer's disease.



Prof Jon Waltho

Gibson Chair in Biophysics

Room: B108
0114 222 2717

Application of multidimensional NMR methods to solving protein structures, complex formation, kinetics, protein molecular recognition and transition states, particularly in kinases.



Prof Mike Williamson

Room: B110
0114 222 4224

Protein structure determination, protein mobility and interactions with ligands by 2D and 3D NMR. Targets include bacterial pathogenesis proteins and human disease-state proteins.