Current Research Interests
Structural Biology Beamline Development
I have had a long-term interest in developments in both hardware and software developments that improve the user experience and access of structural biology beamlines. This supports the science undertaken on macromolecular crystallography beamlines at Diamond Light Source. Projects include the development of:
- MX end-station with new focusing optics and a flexible set-up to allow easy integration of new equipment and techniques.
- Beamline optics to permit rapid, reliable, adjustable beamsizes on demand.
- Exploiting multi-axis goniometry.
- Automated screening and data collection.
- Experimental phasing pipelines.
- Tools for remote access to beamlines and new shift modes.
Structure-function studies of an unusual 3-methyladenine DNA glycosylase II (AlkA) from Deinococcus radiodurans.
E. Moe, D.R. Hall, I. Leiros, V.T. Monsen, J. Timmins and S. McSweeney.
Acta Crystallogr D Biol Crystallogr. 2012 68 703-12.
MxCuBE : a synchrotron beamline control environment customized for macromolecular crystallography experiments.
J. Gabadinho, A. Beteva, M. Guijarro, V. Rey-Bakaikoa, D. Spruce, M.W. Bowler, S. Brockhauser, D. Flot, E.J. Gordon, D.R. Hall, B. Lavault, A.A. McCarthy, J. McCarthy, E. Mitchell, S. Monaco, C. Mueller-Dieckmann, D. Nurizzo, R.B. Ravelli, X. Thibault, M.A. Walsh, G.A. Leonard and S.M. McSweeney.
J Synchrotron Radiat. 2010 17 700-707.
Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.
U. Kapp, S. Macedo, D.R. Hall, I. Leiros, S.M. McSweeney and E. Mitchell.
Acta Crystallogr F Struct Biol Cryst Commun. 2008 64 479-486.
Structural similarity between the DnaA binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli.
G. Natrajan, D.R. Hall, A.C. Thompson, I. Gutsche and L. Terradot.
Mol Microbiol. 2007 65 995-1005.
High-throughput sample handling and data collection at synchrotrons: embedding the ESRF into the high throughput gene-to-structure pipeline.
A. Beteva, F. Cipriani, S. Cusack, S. DeLageniere, J. Gabadinho, E.J. Gordon, M. Guijarro, D.R. Hall, S. Larsen, L. Launer, C.B. Lavault, G.A. Leonard, T. Mairs, A. McCarthy, J. McCarthy, J. Meyer, E. Mitchell, S. Monaco, D. Nurrizo, P. Pernot, R. Pieritz, R.G. Ravelli, V. Rey, W. Shephard, D. Spruce, D.I. Stuart, O. Svennson, P. Theveneau, X. Thibault, J. Turkenburg, M. Walsh and S.M. McSweeney.
Acta Crystallogr D Biol Crystallogr. 2006 62 1162-9.
Communication between subunits within an archaeal clamp-loader complex.
A. Seybert, M.R. Singleton, N. Cook, D.R. Hall and D.B. Wigley
EMBO J. 2006 25 2209–2218.
The care and nurture of undulator data sets.
D. Flot, E.J. Gordon, D.R. Hall, G.A. Leonard, A. McCarthy, J. McCarthy, S. McSweeney, E. Mitchell, D. Nurizzo, R.G. Ravelli, W. Shepard.
Acta Crystallogr D Biol Crystallogr. 2006 62 65-71.
Crystal structure and DNA-binding analysis of RecO from Deinococcus radiodurans.
I. Leiros, J. Timmins, D.R. Hall and S. McSweeney
EMBO J. 2005 24 906-18.
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.
D.R. Hall, L.E. Kemp, G.A. Leonard, K. Marshall, A. Berry and W.N. Hunter
Acta Crystallogr D Biol Crystallogr. 2003 59 611-4.
The mechanism of iron uptake by transferrins: the X-ray structures of the 18 kDa NII domain fragment of duck ovotransferrin and its nitrilotriacetate complex.
P. Kuser, D.R. Hall, M.L. Haw, M. Neu, R.W. Evans and P.F. Lindley.
Acta Crystallogr D Biol Crystallogr. 2002 58 777-83.
The structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism and specificity of class II aldolases.
D.R. Hall, C.S. Bond, G.A. Leonard, C.I. Watt, A. Berry and W.N. Hunter.
J Biol Chem. 2002 277 22018-24.
The crystal and molecular structures of diferric porcine and rabbit serum transferrins at 2.15 and 2.60 Å, respectively.
D.R. Hall, J.M. Hadden, G.A Leonard, S. Bailey, M. Neu, M. Winn and P.F. Lindley.
Acta Crystallogr D Biol Crystallogr. 2002 58 70-80.
RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination.
M.J. McIlwraith, D.R. Hall, A.Z. Stasiak, A. Stasiak, D.B. Wigley and S.C. West.
Nucleic Acids Res. 2001 29 4509-4517.
The three-dimensional structure of a Plasmodium falciparum cyclophilin in complex with the potent anti-malarial cyclosporin A.
M.R. Peterson, D.R. Hall, M. Berriman, J.A. Nunes, G.A. Leonard, A.H. Fairlamb and W.N. Hunter.
J Mol Biol. 2000 298 123-133.
The high resolution crystal structure of the molybdate dependent transcriptional regulator ModE from Escherichia coli.
D.R. Hall, D.G. Gourley, G.A. Leonard, E.M. Duke, L.A. Anderson, D.H. Boxer and W.N. Hunter.
EMBO J. 1999 18 1435-1446.
The crystal structure of Eshecrichia coli class II fructose-1,6-bisphosphate aldolase in complex with phosphogylcolohydroxamate provides information on mechanism and specificity.
D.R. Hall, G.A. Leonard, C.D. Reed, C.I. Watt, A. Berry and W.N. Hunter.
J Mol Biol. 1999 287 383-394.
Two crystal forms of ModE, the molybdate dependent transcriptional regulator from Escherichia coli.
D.R. Hall, D.G. Gourley, E.M. Duke, G.A. Leonard, L.A. Anderson, R.N. Pau, D.H. Boxer and W.N. Hunter.
Acta Crystallogr D Biol Crystallogr. 1999 55 542-543.
Crystallization and preliminary x-ray diffraction studies of 6-phosphogluconate dehydrogenase from Lactococcus lactis.
E. Tetaud, D.R. Hall, D.G. Gourley, G.A. Leonard, S. Arkison, M.P. Barrett and W.N. Hunter.
Acta Crystallogr D Biol Crystallogr. 1998 54 1422-1424.
Dave Hall was appointed Principal Beamline Scientist at Diamond Light Source (DLS) in 2009 after joining Diamond in 2007. Prior to arriving at DLS he spent five years as a beamline scientist in the structural biology group at European Synchrotron Radiation Facility, France, after a post-doctoral position at Cancer Research UK. He undertook a CASE-PhD studentship at the University of Dundee with Prof. Bill Hunter in collaboration with Prof. Peter Lindley at Daresbury Laboratory, where his interest in the use of synchrotron radiation as a tool for investigating structural biology began.