Katherine McAuley

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Katherine McAuley is the Principal Beamline Scientist responsible for beamline I03. She joined Diamond in 2004 from the Synchrotron Radiation Source at Daresbury, UK.

Email: katherine.mcauley@diamond.ac.uk
Tel: +44 (0) 1235 778405

Key Research Area

Key Research Area

  • Handling of pathogenic samples
  • High Throughput Structural Biology
  • Beamline Development

Latest Publications

  1. Automated data collection for macromolecular crystallography. Methods.
  2. A novel technique combining high-resolution synchrotron x-ray microtomography and x-ray diffraction for characterization of micro particulates. Measurement Science & Technology.
  3. Structural Basis of Gate-DNA Breakage and Resealing by Type II Topoisomerases. PLoS One .
  4. Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases. Nature Structural & Molecular Biology.
  5. Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12. J. Biol. Chem.
  1. Research Expertise
  2. Publications
Research Expertise -

Current Research Interests

 

  1. Pathogenic sample handling
  2. Automation developments
  3. In-situ diffraction experiments
Publications - +

Publications

1    Winter, G. & McAuley, K. E. Automated data collection for macromolecular crystallography. Methods 55, 81-93, doi:10.1016/j.ymeth.2011.06.010 (2011).

2    Merrifield, D. R. et al. A novel technique combining high-resolution synchrotron x-ray microtomography and x-ray diffraction for characterization of micro particulates. Measurement Science & Technology 22, doi:11570310.1088/0957-0233/22/11/115703 (2011).

3    Laponogov, I. et al. Structural Basis of Gate-DNA Breakage and Resealing by Type II Topoisomerases. PLoS One 5, doi:e11338 10.1371/journal.pone.0011338 (2010).

4    Duke, E. M. H. et al. in Sri 2009: The 10th International Conference on Synchrotron Radiation Instrumentation Vol. 1234 AIP Conference Proceedings (eds R. Garrett, I. Gentle, K. Nugent, & S. Wilkins)  165-168 (2010).

5    Laponogov, I. et al. Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases. Nature Structural & Molecular Biology 16, 667-669, doi:10.1038/nsmb.1604 (2009).

6    Gloster, T. M. et al. Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12. J. Biol. Chem. 282, 19177-19189, doi:10.1074/jbc.M700224200 (2007).

7    Sorensen, T. L. M., McAuley, K. E., Flaig, R. & Duke, E. M. H. New light for science: synchrotron radiation in structural medicine. Trends in Biotechnology 24, 500-508, doi:10.1016/j.tibteach.2006.09.006 (2006).

8    Cummins, I. et al. Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase. J Mol Biol 359, 422-432, doi:S0022-2836(06)00398-6 [pii]10.1016/j.jmb.2006.03.048 (2006).

9    McAuley, K. E., Svendsen, A., Patkar, S. A. & Wilson, K. S. Structure of a feruloyl esterase from Aspergillus niger. Acta Crystallographica Section D-Biological Crystallography 60, 878-887, doi:10.1107/s0907444904004937 (2004).

10    McAuley, K. E., Cummins, I., Papiz, M., Edwards, R. & Fordham-Skelton, A. P. Purification, crystallization and preliminary X-ray diffraction analysis of S-formylglutathione hydrolase from Arabidopsis thaliana: effects of pressure and selenomethionine substitution on space-group changes. Acta Crystallographica Section D-Biological Crystallography 59, 2272-2274, doi:10.1107/s0907444903020031 (2003).

11    Spiedel, D. et al. Tuning of the optical and electrochemical properties of the primary donor bacteriochlorophylls in the reaction centre from Rhodobacter sphaeroides: spectroscopy and structure. Biochimica Et Biophysica Acta-Bioenergetics 1554, 75-93, doi:Pii s0005-2728(02)00215-3 10.1016/s0005-2728(02)00215-3 (2002).

12    McAuley, K. E. et al. A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN. Acta Crystallographica Section D-Biological Crystallography 57, 1571-1578, doi:10.1107/s090744490101335x (2001).

13    Fyfe, P. K. et al. Probing the interface between membrane proteins and membrane lipids by X-ray crystallography. Trends in Biochemical Sciences 26, 106-112, doi:10.1016/s0968-0004(00)01746-1 (2001).

14    Ridge, J. P. et al. An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre. Biochemical Journal 351, 567-578, doi:10.1042/0264-6021:3510567 (2000).

15    McAuley, K. E. et al. Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center. Biochemistry 39, 15032-15043, doi:10.1021/bi000557r (2000).

16    McAuley, K. E., Fyfe, P. K., Cogdell, R. J., Isaacs, N. W. & Jones, M. R. X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides. Febs Letters 467, 285-290, doi:10.1016/s0014-5793(00)01172-8 (2000).

17    Howard, T. D., McAuley, K. E., Cogdell, R. J. in Membrane Transport (ed S. A. Baldwin) Ch. 11, 269-307 (Oxford University Press, 2000).

18    Fyfe, P. K. et al. Structural consequences of the replacement of glycine M203 with aspartic acid in the reaction center from Rhodobacter sphaeroides. Biochemistry 39, 5953-5960, doi:10.1021/bi9925017 (2000).

19    McAuley, K. E. et al. Structural details of an interaction between cardiolipin and an integral membrane protein. Proceedings of the National Academy of Sciences of the United States of America 96, 14706-14711, doi:10.1073/pnas.96.26.14706 (1999).

20    McAuley-Hecht, K. E. et al. Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: Monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry 37, 4740-4750, doi:10.1021/bi971717a (1998).

21    Fyfe, P. K. et al. Crystallographic studies of mutant reaction centres from Rhodobacter sphaeroides. Photosynthesis Research 55, 133-140, doi:10.1023/a:1006095520441 (1998).

22    Fyfe, P. K., McAuley-Hecht, K. E., Jones, M. R., Cogdell, R. J. in Biomembrane Structures (ed P. I. Haris, Chapman, D.) Ch. 4, 64-87 (IOS Press, 1998).

23    Boggon, T. J. et al. The crystal structure analysis of d(CGCGAASSCGCG)(2), a synthetic DNA dodecamer duplex containing four 4'-thio-2'-deoxythymidine nucleotides. Nucleic Acids Research 24, 951-961, doi:10.1093/nar/24.5.951 (1996).

24    Savva, R., McAuley-Hecht, K., Brown, T. & Pearl, L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373, 487-493, doi:10.1038/373487a0 (1995).

25    Leonard, G. A., McAuley-Hecht, K., Brown, T. & Hunter, W. N. Do C-H...O hydrogen-bonds contribute to the stability of nucleic-acid base-pairs? Acta Crystallographica Section D-Biological Crystallography 51, 136-139, doi:10.1107/s0907444994004713 (1995).

26    McAuley-Hecht, K. E. et al. Crystal-structure of a DNA duplex containing 8-hydroxydeoxyguanine-adenine base-pairs. Biochemistry 33, 10266-10270, doi:10.1021/bi00200a006 (1994).

27    Leonard, G. A. et al. Guanine-1,N-6-ethenoadenine base-pairs in the crystal-structure of d(CGCGAATT(ε-dA)GCG). Biochemistry 33, 4755-4761, doi:10.1021/bi00182a002 (1994).

28    Leonard, G. A. et al. Crystal and molecular-structure of r(CGCGAAUUAGCG) - an RNA duplex containing 2 G(anti).A(anti) base-pairs. Structure 2, 483-494, doi:10.1016/s0969-2126(00)00049-6 (1994).

29    McAuley-Hecht, K. E. & Cooper, A. Microcalorimetry of enzyme-substrate binding: yeast phosphoglycerate kinase. Journal of the Chemical Society, Faraday Transactions 89, 2693-2699 (1993).

30    Leonard, G. A., Hambley, T. W., McAuley-Hecht, K., Brown, T. & Hunter, W. N. Anthracycline DNA interactions at unfavorable base-pair triplet-binding sites - structures of d(CGGCCG) daunomycin and d(TGGCCA) adriamycin complexes. Acta Crystallographica Section D-Biological Crystallography 49, 458-467, doi:10.1107/s090744499300527x (1993).

31    Cooper, A. & McAuley-Hecht, K. E. Microcalorimetry and the Molecular Recognition of Peptides and Proteins. Philosophical Transactions of the Royal Society of London. Series A: Physical and Engineering Sciences 345, 23-35, doi:10.1098/rsta.1993.0114 (1993).