Dr Johan Turkenburg
Office: 01904 328251
X-ray lab: 01904 328274
Email: johan.turkenburg@york.ac.uk
X-ray Facilities Manager (YSBL)
Research Interests
My main interest is the application of crystallographic and cryo-EM techniques to structural studies of biological macromolecules.
I am responsible for the in-house X-ray data collection facilities, and coordinate all aspects of the application for beam time at synchrotron facilities and of synchrotron data collection. I provide crystallographic expertise to many of the research groups within the YSBL, and install, test and make available crystallographic software.
More recently I have also taken on responsibility for the cryo-EM facilities in YSBL. This currently involves sample preparation, grid screening and computing requirements, both software and hardware.
For both X-ray and cryo-EM I provide data and computing management.
I am also the Radiation Protection Supervisor for X-ray generators in the Departments of Chemistry and Biology.
I am heavily involved in formulating the requirements for the housing and installation of the Cryo Electron Microscope, along with the X-ray equipment and NMR, and making sure that as the building work progresses, the facilities will meet our requirements upon completion in summer 2020.
External activities
Co-organiser of the CCP4/BCA Protein Crystallography Summer School 2019 at York (with Dr. Tracey Gloster) attended by 52 students
Co-organiser of the CCP4/BCA Protein Crystallography Summer School 2017 at St Andrews (with Dr. Tracey Gloster) attended by 45 students
Member of the User Working Group for the in-situ beamline VMXi at Diamond Light Source
Member of the User Working Group for the Long wavelength beamline I23 at Diamond Light Source
Member of the Diamond User Committee for the MX Village (2009-2011)
Scientific organiser (with Dr. Katherine McCauley, Diamond Light Source) CCP4 Study Weekend 2005 "Data collection and processing"
Scientific organiser (with Prof. Leo Brady, Bristol) CCP4 Study Weekend 1999 "Data collection and processing"
Selected Publications
For a full list of publications see http://orcid.org/0000-0001-6992-6838
1. Defining the remarkable structural malleability of a bacterial surface protein Rib domain implicated in infection. Whelan, F., Lafita, A., Griffiths, S. C., Cooper, R. E. M., Whittingham, J. L., Turkenburg, J. P., Manfield, I. W., John, A. N. S., Paci, E., Bateman, A. & Potts, J. R. (2019), P Natl Acad Sci USA 116, 26540-26548.
2. A family of native amine dehydrogenases for the asymmetric reductive amination of ketones. Mayol, O., Bastard, K., Beloti, L., Frese, A., Turkenburg, J. P., Petit, J. L., Mariage, A., Debard, A., Pellouin, V., Perret, A., de Berardinis, V., Zaparucha, A., Grogan, G. & Vergne-Vaxelaire, C. (2019), Nat Catal 2, 324-333.
3. Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Roed, N. K., Viola, C. M., Kristensen, O., Schluckebier, G., Norrman, M., Sajid, W., Wade, J. D., Andersen, A. S., Kristensen, C., Ganderton, T. R., Turkenburg, J. P., De Meyts, P. & Brzozowski, A. M. (2018), Nature Communications 9.
4. Structural and functional insights into asymmetric enzymatic dehydration of alkenols. Nestl, B. M., Geinitz, C., Popa, S., Rizek, S., Haselbeck, R. J., Stephen, R., Noble, M. A., Fischer, M. P., Ralph, E. C., Hau, H. T., Man, H., Omar, M., Turkenburg, J. P., van Dien, S., Culler, S. J., Grogan, G. & Hauer, B. (2017), Nature Chemical Biology 13, 275-+.
5. Bacteria in an intense competition for iron: Key component of the Campylobacter jejuni iron uptake system scavenges enterobactin hydrolysis product. Raines, D. J., Moroz, O., Blagova, E. V., Turkenburg, J. P., Wilson, K. S. & Duhme-Klair, A. K. (2016), P Natl Acad Sci USA 113, 5850-5855.
6. Activity, stability and 3-D structure of the Cu(II) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens. Gregory, R. C., Hemsworth, G. R., Turkenburg, J. P., Hart, S. J., Walton, P. H. & Davies, G. J. (2016), Dalton T 45, 16904-16912.
