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A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from <em>Streptomyces lividans</em>
Lučić, M., Chaplin, A. K., Moreno-Chicano, T., Dworkowski, F. S. N., Wilson, M. T., Svistunenko, D. A., … Worrall, J. A. R. (2020). A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from Streptomyces lividans. Dalton Transactions, 49(5), 1620-1636. https://doi.org/10.1039/c9dt04583j
Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography
Weinert, T., Skopintsev, P., James, D., Dworkowski, F., Panepucci, E., Kekilli, D., … Standfuss, J. (2019). Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science, 365(6448), 61-65. https://doi.org/10.1126/science.aaw8634
Enzyme catalysis captured using multiple structures from one crystal at varying temperatures
Horrell, S., Kekilli, D., Sen, K., Owen, R. L., Dworkowski, F. S. N., Antonyuk, S. V., … Hough, M. A. (2018). Enzyme catalysis captured using multiple structures from one crystal at varying temperatures. IUCrJ, 5(3), 283-292. https://doi.org/10.1107/S205225251800386X
High-intensity x-ray microbeam for macromolecular crystallography using silicon kinoform diffractive lenses
Lebugle, M., Dworkowski, F., Pauluhn, A., Guzenko, V. A., Romano, L., Meier, N., … David, C. (2018). High-intensity x-ray microbeam for macromolecular crystallography using silicon kinoform diffractive lenses. Applied Optics, 57(30), 9032-9039. https://doi.org/10.1364/AO.57.009032
Engineering proximal vs. distal heme-NO coordination via dinitrosyl dynamics: implications for NO sensor design
Kekilli, D., Petersen, C. A., Pixton, D. A., Ghafoor, D. D., Abdullah, G. H., Dworkowski, F. S. N., … Hough, M. A. (2017). Engineering proximal vs. distal heme-NO coordination via dinitrosyl dynamics: implications for NO sensor design. Chemical Science, 8(3), 1986-1994. https://doi.org/10.1039/c6sc04190f
Photoreduction and validation of haem-ligand intermediate states in protein crystals by <em>in situ</em> single-crystal spectroscopy and diffraction
Kekilli, D., Moreno-Chicano, T., Chaplin, A. K., Horrell, S., Dworkowski, F. S. N., Worrall, J. A. R., … Hough, M. A. (2017). Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction. IUCrJ, 4, 263-270. https://doi.org/10.1107/S2052252517002159
Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons
Weinert, T., Olieric, N., Cheng, R., Brünle, S., James, D., Ozerov, D., … Standfuss, J. (2017). Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nature Communications, 8(1), 542 (11 pp.). https://doi.org/10.1038/s41467-017-00630-4
Serial millisecond crystallography of membrane proteins
Jaeger, K., Dworkowski, F., Nogly, P., Milne, C., Wang, M., & Standfuss, J. (2016). Serial millisecond crystallography of membrane proteins. In I. Moraes (Ed.), Advances in experimental medicine and biology: Vol. 922. The next generation in membrane protein structure determination. https://doi.org/10.1007/978-3-319-35072-1_10
Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams
Botha, S., Nass, K., Barends, T., Kabsch, W., Latz, B., Dworkowski, F., … Doak, R. B. (2015). Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams. Acta Crystallographica Section D: Structural Biology, 71, 387-397. https://doi.org/10.1107/S1399004714026327
Challenges and solutions for the analysis of <i>in situ, in crystallo</i> micro-spectrophotometric data
Dworkowski, F. S. N., Hough, M. A., Pompidor, G., & Fuchs, M. R. (2015). Challenges and solutions for the analysis of in situ, in crystallo micro-spectrophotometric data. Acta Crystallographica Section D: Structural Biology, 71, 27-35. https://doi.org/10.1107/S1399004714015107
Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'
Ghafoor, D. D., Kekilli, D., Abdullah, G. H., Dworkowski, F. S. N., Hassan, H. G., Wilson, M. T., … Hough, M. A. (2015). Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'. Journal of Biological Inorganic Chemistry, 20(6), 949-956. https://doi.org/10.1007/s00775-015-1278-y
Conformational transitions driven by pyridoxal-5′-phosphate uptake in the psychrophilic serine hydroxymethyltransferase from &lt;em&gt;Psychromonas ingrahamii&lt;/em&gt;
Angelaccio, S., Dworkowski, F., Di Bello, A., Milano, T., Capitani, G., & Pascarella, S. (2014). Conformational transitions driven by pyridoxal-5′-phosphate uptake in the psychrophilic serine hydroxymethyltransferase from Psychromonas ingrahamii. Proteins, 82(10), 2831-2841. https://doi.org/10.1002/prot.24646
Human cellular retinaldehyde-binding protein has secondary thermal 9-<i>cis</i>-retinal isomerase activity
Bolze, C. S., Helbling, R. E., Owen, R. L., Pearson, A. R., Pompidor, G., Dworkowski, F., … Stocker, A. (2014). Human cellular retinaldehyde-binding protein has secondary thermal 9-cis-retinal isomerase activity. Journal of the American Chemical Society, 136(1), 137-146. https://doi.org/10.1021/ja411366w
D3, the new diffractometer for the macromolecular crystallography beamlines of the Swiss Light Source
Fuchs, M. R., Pradervand, C., Thominet, V., Schneider, R., Panepucci, E., Grunder, M., … Wang, M. (2014). D3, the new diffractometer for the macromolecular crystallography beamlines of the Swiss Light Source. Journal of Synchrotron Radiation, 21(2), 340-351. https://doi.org/10.1107/S160057751400006X
Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy
Kekilli, D., Dworkowski, F. S. N., Pompidor, G., Fuchs, M. R., Andrew, C. R., Antonyuk, S., … Hough, M. A. (2014). Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy. Acta Crystallographica Section D: Structural Biology, 70(5), 1289-1296. https://doi.org/10.1107/S1399004714004039
Selective X-ray-induced NO photodissociation in haemoglobin crystals: Evidence from a Raman-assisted crystallographic study
Merlino, A., Fuchs, M. R., Pica, A., Balsamo, A., Dworkowski, F. S. N., Pompidor, G., … Vergara, A. (2013). Selective X-ray-induced NO photodissociation in haemoglobin crystals: Evidence from a Raman-assisted crystallographic study. Acta Crystallographica Section D: Structural Biology, 69(1), 137-140. https://doi.org/10.1107/S0907444912042229
A new on-axis micro-spectrophotometer for combining Raman, fluorescence and UV/Vis absorption spectroscopy with macromolecular crystallography at the Swiss Light Source
Pompidor, G., Dworkowski, F. S. N., Thominet, V., Schulze-Briese, C., & Fuchs, M. R. (2013). A new on-axis micro-spectrophotometer for combining Raman, fluorescence and UV/Vis absorption spectroscopy with macromolecular crystallography at the Swiss Light Source. Journal of Synchrotron Radiation, 20(5), 765-776. https://doi.org/10.1107/S0909049513016063
Radiation damage in room-temperature data acquisition with the PILATUS 6M pixel detector
Rajendran, C., Dworkowski, F. S. N., Wang, M., & Schulze-Briese, C. (2011). Radiation damage in room-temperature data acquisition with the PILATUS 6M pixel detector. Journal of Synchrotron Radiation, 18(3), 318-328. https://doi.org/10.1107/S090904951100968X