Byron, Olwyn - University of Glasgow - School of Life Sciences

研究领域

We specialise in understanding the solution behaviour of biological macromolecules and their complexes. We do this by utilising a number of biophysical techniques to determine the solution shape of molecules and the strength, stoichiometry and architecture of the complexes they form. We collaborate widely and offer expertise in the application of our core methodologies including: Analytical ultracentrifugation (AUC) Small angle X-ray scattering (SAXS) Small angle neutron scattering (SANS) Hydrodynamic bead modelling (HBM)

近期论文

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Grinter, R. et al. (2016) Structure of the bacterial plant-ferredoxin receptor FusA. Nature Communications, 7, 13308. (doi:10.1038/ncomms13308) (PMID:27796364) Klein, A., Wojdyla, J. A., Joshi, A., Josts, I., McCaughey, L. C., Housden, N. G., Kaminska, R., Byron, O., Walker, D., and Kleanthous, C. (2016) Structural and biophysical analysis of nuclease protein antibiotics. Biochemical Journal, 473(18), pp. 2799-2812. (doi:10.1042/bcj20160544) (PMID:27402794) (PMCID:PMC5264503) Mccaughey, L. C., Josts, I., Grinter, R., White, P., Byron, O., Tucker, N. P., Matthews, J. M., Kleanthous, C., Whitchurch, C., and Walker, D. (2016) Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa. Biochemical Journal, 473(15), pp. 2345-2358. (doi:10.1042/bcj20160470) (PMID:27252387) (PMCID:PMC4964976) Ashraf, K. U., Josts, I., Mosbahi, K., Kelly, S. M., Byron, O., Smith, B. O., and Walker, D. (2016) The potassium binding protein Kbp is a cytoplasmic potassium sensor. Structure, 24(5), pp. 741-749. (doi:10.1016/j.str.2016.03.017) (PMID:27112601) Byron, O., and Vestergaard, B. (2015) Protein–protein interactions: a supra-structural phenomenon demanding trans-disciplinary biophysical approaches. Current Opinion in Structural Biology, 35, pp. 76-86. (doi:10.1016/j.sbi.2015.09.003) Rocco, M., and Byron, O. (2015) Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs. European Biophysics Journal, 44(6), pp. 417-431. (doi:10.1007/s00249-015-1042-9) Rocco, M., and Byron, O. (2015) Erratum to: Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs. European Biophysics Journal, 44(6), pp. 433-436. (doi:10.1007/s00249-015-1058-1) (PMID:26187588) Joshi, A. et al. (2015) Structures of the ultra-high-affinity protein–protein complexes of pyocins S2 and AP41 and their cognate immunity proteins from pseudomonas aeruginosa. Journal of Molecular Biology, 427(17), pp. 2852-2866. (doi:10.1016/j.jmb.2015.07.014) (PMID:26215615) (PMCID:PMC4548480) Fyfe, C.D., Grinter, R., Josts, I., Mosbahi, K., Roszak, A.W., Cogdell, R.J., Wall, D.M., Burchmore, R.J.S., Byron, O., and Walker, D. (2015) Structure of protease-cleaved escherichia coliα-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment. Acta Crystallographica. Section D: Biological Crystallography, 71(7), pp. 1478-1486. (doi:10.1107/s1399004715008548) (PMID:26143919) (PMCID:PMC4498604) Rocco, M., and Byron, O. (2015) Hydrodynamic modeling and its application in AUC. Methods in Enzymology, 562, pp. 81-108. (doi:10.1016/bs.mie.2015.04.010) (PMID:26412648) Zhao, H. et al. (2015) A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. PLoS ONE, 10(5), e0126420. (doi:10.1371/journal.pone.0126420) (PMID:25997164) (PMCID:PMC4440767) English, G., Byron, O., Cianfanelli, F. R., Prescott, A. R., and Coulthurst, S. J. (2014) Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK–TssFG subcomplex. Biochemical Journal, 461(2), pp. 291-304. (doi:10.1042/BJ20131426) Beckham, K. S.H. et al. (2014) The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7. Molecular Microbiology, 93(1), pp. 199-211. (doi:10.1111/mmi.12651) (PMID:24846743) (PMCID:PMC4249723) Grinter, R., Josts, I., Zeth, K., Roszak, A. W., McCaughey, L. C., Cogdell, R. J., Milner, J. J., Kelly, S. M., Byron, O., and Walker, D. (2014) Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake. Molecular Microbiology, 93(2), pp. 234-246. (doi:10.1111/mmi.12655) Mccaughey, L. C. et al. (2014) Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. PLoS Pathogens, 10(2), e1003898. (doi:10.1371/journal.ppat.1003898) Dow, J.M., Grahl, S., Ward, R., Evans, R., Byron, O., Norman, D.G., Palmer, T., and Sargent, F. (2014) Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. FEBS Journal, 281(1), pp. 246-260. (doi:10.1111/febs.12592) Josts, I., Grinter, R., Kelly, S. M., Mosbahi, K., Roszak, A., Cogdell, R., Smith, B. O., Byron, O., and Walker, D. (2014) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963–1138 domain of TamB from Escherichia coli. Acta Crystallographica. Section F: Structural Biology Communications, 70(9), pp. 1272-1275. (doi:10.1107/S2053230X14017403) Laine, L. M., Biddau, M., Byron, O., and Müller, S. (2014) Biochemical and structural characterisation of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparum. Bioscience Reports, 35(1), e00171. (doi:10.1042/BSR20140150) (PMID:25387830) (PMCID:PMC4293902) Beckham, K. S.H., Byron, O., Roe, A. J., and Gabrielsen, M. (2012) The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(5), pp. 522-526. (doi:10.1107/S1744309112011487) (PMID:22691780) (PMCID:PMC3374505) Gabrielsen, M., Beckham, K.S., Feher, V.A., Zetterstrom, C.E., Wang, D., Muller, S., Elofsson, M., Amaro, R.E., Byron, O., and Roe, A.J. (2012) Structural characterisation of Tpx from yersinia pseudotuberculosis reveals insights into the binding of salicylidene acylhydrazide compounds. PLoS ONE, 7(2), e32217. (doi:10.1371/journal.pone.0032217) Gabrielsen, M., Beckham, K.S.H., Cogdell, R.J., Byron, O., and Roe, A.J. (2012) FolX from Pseudomonas aeruginosa is octameric in both crystal and solution. FEBS Letters, 586(8), pp. 1160-1165. (doi:10.1016/j.febslet.2012.03.031) Rasmussen, L.C.V., Oliveira, C.L.P., Byron, O., Jensen, J.M., Pedersen, J.S., Sperling-Petersen, H.U., and Mortensen, K.K. (2011) Structure and dimerization of translation initiation factor aIF5B in solution. Biochemical and Biophysical Research Communications, 416(1-2), pp. 140-145. (doi:10.1016/j.bbrc.2011.11.012) Wang, D. et al. (2011) Identification of bacterial target proteins for the salicylidene acylhydrazide class of virulence blocking compounds. Journal of Biological Chemistry, 286(34), pp. 29922-29931. (doi:10.1074/jbc.M111.233858) Vijayakrishnan, S., Callow, P., Nutley, M.A., McGow, D.P., Kropholler, P., Cooper, A., Byron, O., and Lindsay, J.G. (2011) Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly. Biochemical Journal, 437(3), pp. 565-574. (doi:10.1042/BJ20101784) Moore, V., Kanu, A., Byron, O., Campbell, G., Danson, M.J., Hough, D.J., and Crennell, S.J. (2011) Contribution of inter-subunit interactions to the thermostability of Pyrococcus furiosus citrate synthase. Extremophiles, 15(3), pp. 327-336. (doi:10.1007/s00792-011-0363-6)