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In meso in situ serial X-Ray crystallography (IMISX): a protocol for membrane protein structure determination at the Swiss Light Source
Huang, C. Y., Olieric, V., Caffrey, M., & Wang, M. (2020). In meso in situ serial X-Ray crystallography (IMISX): a protocol for membrane protein structure determination at the Swiss Light Source. In C. Perez & T. Maier (Eds.), Methods in molecular biology: Vol. 2127. Expression, purification, and structural biology of membrane proteins. https://doi.org/10.1007/978-1-0716-0373-4_20
JUNGFRAU detector for brighter x-ray sources: solutions for IT and data science challenges in macromolecular crystallography
Leonarski, F., Mozzanica, A., Brückner, M., Lopez-Cuenca, C., Redford, S., Sala, L., … Wang, M. (2020). JUNGFRAU detector for brighter x-ray sources: solutions for IT and data science challenges in macromolecular crystallography. Structural Dynamics, 7(1), 014305 (13 pp.). https://doi.org/10.1063/1.5143480
X-ray fluorescence detection for serial macromolecular crystallography using a JUNGFRAU pixel detector
Martiel, I., Mozzanica, A., Opara, N. L., Panepucci, E., Leonarski, F., Redford, S., … Wang, M. (2020). X-ray fluorescence detection for serial macromolecular crystallography using a JUNGFRAU pixel detector. Journal of Synchrotron Radiation, 27, 329-339. https://doi.org/10.1107/S1600577519016758
Characterization of a toxin-antitoxin system in <em>Mycobacterium tuberculosis</em> suggests neutralization by phosphorylation as the antitoxicity mechanism
Yu, X., Gao, X., Zhu, K., Yin, H., Mao, X., Wojdyla, J. A., … Cui, S. (2020). Characterization of a toxin-antitoxin system in Mycobacterium tuberculosis suggests neutralization by phosphorylation as the antitoxicity mechanism. Communications Biology, 3(1), 216 (15 pp.). https://doi.org/10.1038/s42003-020-0941-1
Automated data collection and real-time data analysis suite for serial synchrotron crystallography
Basu, S., Kaminski, J. W., Panepucci, E., Huang, C. Y., Warshamanage, R., Wang, M., & Wojdyla, J. A. (2019). Automated data collection and real-time data analysis suite for serial synchrotron crystallography. Journal of Synchrotron Radiation, 26(1), 244-252. https://doi.org/10.1107/S1600577518016570
Long-wavelength native-SAD phasing: opportunities and challenges
Basu, S., Olieric, V., Leonarski, F., Matsugaki, N., Kawano, Y., Takashi, T., … Wang, M. (2019). Long-wavelength native-SAD phasing: opportunities and challenges. IUCrJ, 6(3), 1-14. https://doi.org/10.1107/S2052252519002756
Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source
Basu, S., Finke, A., Vera, L., Wang, M., & Olieric, V. (2019). Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source. Acta Crystallographica Section D: Structural Biology, 75(3), 262-271. https://doi.org/10.1107/S2059798319003103
Crystal structure of a natural light-gated anion channelrhodopsin
Li, H., Huang, C. Y., Govorunova, E. G., Schafer, C. T., Sineshchekov, O. A., Wang, M., … Spudich, J. L. (2019). Crystal structure of a natural light-gated anion channelrhodopsin. eLife, 8, e41741 (21 pp.). https://doi.org/10.7554/eLife.41741
Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules
Liu, X., An, T., Li, D., Fan, Z., Xiang, P., Li, C., … Peng, X. (2019). Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules. Proceedings of the National Academy of Sciences of the United States of America PNAS, 116(6), 2068-2077. https://doi.org/10.1073/pnas.1810969116
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
Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
El Ghachi, M., Howe, N., Huang, C. Y., Olieric, V., Warshamanage, R., Touzé, T., … Caffrey, M. (2018). Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nature Communications, 9(1), 1078 (13 pp.). https://doi.org/10.1038/s41467-018-03477-5
Structural insight into conformational changes induced by ATP binding in a type III secretion-associated ATPase from <em>Shigella flexneri</em>
Gao, X., Mu, Z., Yu, X., Qin, B., Wojdyla, J., Wang, M., & Cui, S. (2018). Structural insight into conformational changes induced by ATP binding in a type III secretion-associated ATPase from Shigella flexneri. Frontiers in Microbiology, 9, 1468 (15 pp.). https://doi.org/10.3389/fmicb.2018.01468
In situ serial crystallography for rapid de novo membrane protein structure determination.
Huang, C. Y., Olieric, V., Howe, N., Warshamanage, R., Weinert, T., Panepucci, E., … Wang, M. (2018). In situ serial crystallography for rapid de novo membrane protein structure determination. Communications Biology, 1, 124 (8 pp.). https://doi.org/10.1038/S42003-018-0123-6
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
Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector
Leonarski, F., Redford, S., Mozzanica, A., Lopez-Cuenca, C., Panepucci, E., Nass, K., … Wang, M. (2018). Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector. Nature Methods, 15(10), 799-804. https://doi.org/10.1038/s41592-018-0143-7
Practical approaches for in situ X-ray crystallography: from high-throughput screening to serial data collection
Martiel, I., Olieric, V., Caffrey, M., & Wang, M. (2018). Practical approaches for in situ X-ray crystallography: from high-throughput screening to serial data collection. In K. Beis & G. Evans (Eds.), Chemical biology: Vol. 8. Protein crystallography: challenges and practical solutions. https://doi.org/10.1039/9781788010504-00001
Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals
Opara, N. L., Mohacsi, I., Makita, M., Castano-Diez, D., Diaz, A., Juranić, P., … David, C. (2018). Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals. Structural Dynamics, 5(5), 054303 (15 pp.). https://doi.org/10.1063/1.5050618
Structural characterization of free-state and product-state <i>Mycobacterium tuberculosis</i> methionyl-tRNA synthetase reveals an induced-fit ligand-recognition mechanism
Wang, W., Qin, B., Wojdyla, J. A., Wang, M., Gao, X., & Cui, S. (2018). Structural characterization of free-state and product-state Mycobacterium tuberculosis methionyl-tRNA synthetase reveals an induced-fit ligand-recognition mechanism. IUCrJ, 5, 478-490. https://doi.org/10.1107/S2052252518008217
&lt;em&gt;DA+&lt;/em&gt; data acquisition and analysis software at the Swiss Light Source macromolecular crystallography beamlines
Wojdyla, J. A., Kaminski, J. W., Panepucci, E., Ebner, S., Wang, X., Gabadinho, J., & Wang, M. (2018). DA+ data acquisition and analysis software at the Swiss Light Source macromolecular crystallography beamlines. Journal of Synchrotron Radiation, 25(1), 293-303. https://doi.org/10.1107/S1600577517014503
Crystal structure of the human 5-HT&lt;sub&gt;1B&lt;/sub&gt; serotonin receptor bound to an inverse agonist
Yin, W., Zhou, X. E., Yang, D., de Waal, P. W., Wang, M., Dai, A., … Jiang, Y. (2018). Crystal structure of the human 5-HT1B serotonin receptor bound to an inverse agonist. Cell Discovery, 4, 12 (13 pp.). https://doi.org/10.1038/s41421-018-0009-2
 

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