CV
2006 Beamline scientist, Swiss Light Source, Villigen-PSI, Switzerland
2001 Ph.D. University of Alberta, Edmonton, Canada
Research interests
My main research interests are in macromolecular crystallography (MX) beamline instrumentation and methods development and their applications in both academic and proprietary research.
1. MX beamline development. We use a science-driven and instrumentation-inspired approach in beamline development. We exploited two-stage dynamic focusing to fully control the size and divergence of X-rays, implemented multi-axis goniometers to improve data accuracy (b), developed advanced X-ray detectors to record diffraction with the highest precision and accuracy (a,c,f), and automated fast sample exchange (g) and X-ray data collection (d,e). Collectively, three SLS MX beamlines have delivered 7200 structures to date, which makes them the most productive MX beamlines worldwide (http://biosync.sbkb.org/).
a. Mueller, M., Wang, M. & Schulze-Briese, C. Optimal fine φ-slicing for single-photon-counting pixel detectors. Acta Crystallogr. D Biol. Crystallogr. 68, 42–56 (2012).
b. Waltersperger, S. et al. PRIGo: a new multi-axis goniometer for macromolecular crystallography. J. Synchrotron Radiat. 22, 895–900 (2015).
c. Casanas, A. et al. EIGER detector: application in macromolecular crystallography. Acta Crystallogr D Struct Biol 72, 1036–1048 (2016).
d. Wojdyla, J. A. et al. Fast two-dimensional grid and transmission X-ray microscopy scanning methods for visualizing and characterizing protein crystals. J. Appl. Crystallogr. 49, 944–952 (2016).
e. Wojdyla, J. A. et al. DA+ data acquisition and analysis software at the Swiss Light Source macromolecular crystallography beamlines. J. Synchrotron Radiat. 25, 293–303 (2018).
f. Leonarski, F. et al. Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector. Nat. Methods 15, 799–804 (2018).
g. Martiel, I. et al. The TELL automatic sample changer for macromolecular crystallography. J. Synchrotron Radiat. 27, 860-863 (2020).
2. Experimental phasing. We pioneered the low-dose multi-orientation data collection strategy for native-SAD phasing in 2014 (a,b). This method enables de novo structure determination from native biomolecules without labeling and derivatization and has been widely used in many synchrotron facilities since then (c). Currently we are push the frontier to low-energy X-rays aiming to solve the crystallographic phase problem experimentally (d).
a. Weinert, T. et al. Fast native-SAD phasing for routine macromolecular structure determination. Nat. Methods 12, 131–133 (2015).
b. Olieric, V. et al. Data-collection strategy for challenging native SAD phasing. Acta Crystallogr D Struct Biol 72, 421–429 (2016).
c. Finke, A. D. et al. Advanced Crystallographic Data Collection Protocols for Experimental Phasing. Methods Mol. Biol. 1320, 175–191 (2016).
d. Basu, S. et al. Long-wavelength native-SAD phasing: opportunities and challenges. IUCrJ 6, 373–386 (2019)
3. In situ serial synchrotron crystallography. One main bottleneck in membrane structure determination with in meso method is the crystal harvesting, which is a tedious, time-consuming, and low-efficiency process and often damages the valuable crystals. With collaborators, I led an innovative method development to enable in situ X-ray data collection with crystals in their growth environment in a serial manner (a,b,e). The new method is termed as in meso in situ serial crystallography (IMISX) and has been applied successfully for a broad range of membrane proteins (c,d,f). The method has been further improved with 3D-printed sample holders recently (g).
a. Huang, C. Y. et al. In meso in situ serial X-ray crystallography of soluble and membrane proteins. Acta Crystallogr. D Biol. Crystallogr. 71, 1238–1256 (2015).
b. Huang, C. Y. et al. In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures. Acta Crystallogr D Struct Biol 72, 93–112 (2016).
c. Diederichs, K. & Wang, M. Serial Synchrotron X-Ray Crystallography (SSX). Methods Mol. Biol. 1607, 239–272 (2017).
d. El Ghachi, M. et al. Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nat. Commun. 9, 1078 (2018).
e. Huang, C.-Y. et al. In situ serial crystallography for rapid de novo membrane protein structure determination. Commun Biol 1, 124 (2018).
f. Huang, C.-Y. et al. In Meso In Situ Serial X-Ray Crystallography (IMISX): A Protocol for Membrane Protein Structure Determination at the Swiss Light Source. Methods Mol. Biol. 2127, 293–319 (2020).
g. Huanf, C.-Y. et al. 3D-printed holders for in meso in situ fixed-target serial X-ray crystallography. J. Appl. Crystallogr. In press.
4. Time-resolved serial synchrotron crystallography. Development of injector-based serial synchrotron crystallography for room-temperature structure determination and dynamics study (a). We have demonstrated that room-temperature structures can be determined from microcrystals by a combined use of LCP injector, micro-focused X-ray beam and fast frame-rate detectors (PILATUS and EIGER) (b). We also revived time-resolved synchrotron crystallography with a serial crystallography approach recently (c).
a. Botha, S. et al. Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams. Acta Crystallogr. D Biol. Crystallogr. 71, 387–397 (2015).
b. Weinert, T. et al. Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nat. Commun. 8, 542 (2017).
c. Weinert, T. et al. Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science 365, 61–65 (2019).
Publications
* corresponding author
114. Gao, X., Qin, B., Chen, P., Zhu, K., Hou, P., Wojdyla, J. A., Wang, M. & Cui, S. Crystal structure of SARS-CoV-2 papain-like protease. Acta Pharm Sin B (2020). doi:10.1016/j.apsb.2020.08.014
113. Martiel, I., Huang, C.-Y., Villanueva-Perez, P., Panepucci, E., Basu, S., Caffrey, M., Pedrini, B., Bunk, O., Stampanoni, M. & Wang, M.* Low-dose in situ prelocation of protein microcrystals by 2D X-ray phase-contrast imaging for serial crystallography. IUCrJ 7, 1131–1141 (2020).
112. Nass, K., Cheng, R., Vera, L., Mozzanica, A., Redford, S., Ozerov, D., Basu, S., James, D., Knopp, G., Cirelli, C., Martiel, I., Casadei, C., Weinert, T., Nogly, P., Skopintsev, P., Usov, I., Leonarski, F., Geng, T., Rappas, M., Doré, A. S., Cooke, R., Nasrollahi Shirazi, S., Dworkowski, F., Sharpe, M., Olieric, N., Bacellar, C., Bohinc, R., Steinmetz, M. O., Schertler, G., Abela, R., Patthey, L., Schmitt, B., Hennig, M., Standfuss, J., Wang, M.* & Milne, C. J. Advances in long-wavelength native phasing at X-ray free-electron lasers. IUCrJ 7, 965–975 (2020).
111. Assmann, G. M., Wang, M. & Diederichs, K. Making a difference in multi-data-set crystallography: simple and deterministic data-scaling/selection methods. Acta Crystallogr D Struct Biol 76, 636–652 (2020).
110. Bu, W., Levitskaya, Z., Loh, Z. Y., Jin, S., Basu, S., Ero, R., Yan, X., Wang, M., Ngan, S. F. C., Sze, S. K., Tan, S.-M. & Gao, Y.-G. Structural basis of human full-length kindlin-3 homotrimer in an auto-inhibited state. PLoS Biol. 18, e3000755 (2020).
109. Huang, C.-Y., Meier, N., Caffrey, M., Wang, M. & Olieric, V. 3D-printed holders for in meso in situ fixed-target serial X-ray crystallography. J. Appl. Crystallogr. 53, 854–859 (2020).
108. Gao, X., Zhu, K., Wojdyla, J. A., Chen, P., Qin, B., Li, Z., Wang, M.* & Cui, S.* Crystal structure of the NS3-like helicase from Alongshan virus. IUCrJ 7, 375 (2020).
107. Yu, X., Gao, X., Zhu, K., Yin, H., Mao, X., Wojdyla, J. A., Qin, B., Huang, H., Wang, M., Sun, Y.-C. & Cui, S. Characterization of a toxin-antitoxin system in Mycobacterium tuberculosis suggests neutralization by phosphorylation as the antitoxicity mechanism. Commun Biol 3, 216 (2020).
106. Martiel, I.*, Buntschu, D., Meier, N., Gobbo, A., Panepucci, E., Schneider, R., Heimgartner, P., Müller, D., Bühlmann, K., Birri, M., Kaminski, J. W., Leuenberger, J., Oliéric, V., Glettig, W. & Wang, M.* The TELL automatic sample changer for macromolecular crystallography. J. Synchrotron Radiat. 27, 860 (2020).
105. Martiel, I., Mozzanica, A., Opara, N. L., Panepucci, E., Leonarski, F., Redford, S., Mohacsi, I., Guzenko, V., Ozerov, D., Padeste, C., Schmitt, B., Pedrini, B. & Wang, M.* X-ray fluorescence detection for serial macromolecular crystallography using a JUNGFRAU pixel detector. J. Synchrotron Radiat. 27, 329 (2020).
104. Leonarski, F.*, Mozzanica, A., Brückner, M., Lopez-Cuenca, C., Redford, S., Sala, L., Babic, A., Billich, H., Bunk, O., Schmitt, B. & Wang, M. JUNGFRAU detector for brighter x-ray sources: Solutions for IT and data science challenges in macromolecular crystallography. Struct Dyn 7, 014305 (2020).
103. Huang, C.-Y., Olieric, V., Caffrey, M. & Wang, M.* In Meso In Situ Serial X-Ray Crystallography (IMISX): A Protocol for Membrane Protein Structure Determination at the Swiss Light Source. Methods Mol. Biol. 2127, 293 (2020).
102. Weinert, T.*, Skopintsev, P., James, D., Dworkowski, F., Panepucci, E., Kekilli, D., Furrer, A., Brünle, S., Mous, S., Ozerov, D., Nogly, P., Wang, M. & Standfuss, J. Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science 365, 61 (2019).
101. Basu S., Olieric V., Leonarski F., Matsugaki N., Kawano Y., Takashi T., Huang C.-Y., Yamada Y., Vera L., Olieric N., Basquin J., Wojdyla J. A., Bunk O., Diederichs K., Yamamoto M., Wang M.* Long-wavelength native-SAD phasing: opportunities and challenges. IUCrJ 6, 373 (2019).
100. Basu S., Finke A., Vera L., Wang M., Olieric V. Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source. Acta Crystallogr. D Struct. Biol. 75, 262 (2019).
99. Liu X., An T., Li D., Fan Z., Xiang P., Li C., Ju W., Li J., Hu G., Qin B., Yin B., Wojdyla J. A., Wang M., Yuan J., Qiang B., Shu P., Cui S., Peng X. Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules. Proc. Natl. Acad. Sci. U S A 116, 2068 (2019).
98. Li H., Huang C.-Y., Govorunova E. G., Schafer C. T., Sineshchekov O. A., Wang M., Zheng L., Spudich J. L. Crystal structure of a natural light-gated anion channelrhodopsin. Elife 8, doi: 10.7554/eLife.41741 (2019).
97. Basu S., Kaminski J. W., Panepucci E., Huang C.-Y., Warshamanage R., Wang M., Wojdyla J. A. Automated data collection and real-time data analysis suite for serial synchrotron crystallography. J. Synchrotron Radiat. 26, 244 (2019).
96. Lebugle M., Dworkowski F., Pauluhn A., Guzenko V. A., Romano L., Meier N., Marschall F., Sanchez D. F., Grolimund D., Wang M., David C. High-intensity x-ray microbeam for macromolecular crystallography using silicon kinoform diffractive lenses. Appl. Opt. 57, 9032 (2018).
95. Leonarski F., Redford S., Mozzanica A., Lopez-Cuenca C., Panepucci E., Nass K., Ozerov D., Vera L., Olieric V., Buntschu D., Schneider R., Tinti G., Froejdh E., Diederichs K., Bunk O., Schmitt B., Wang M.* Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector. Nat. Methods 15, 799 (2018).
94. Opara N. L., Mohacsi I., Makita M., Castano-Diez D., Diaz A., Juranić P., Marsh M., Meents A., Milne C. J., Mozzanica A., Padeste C., Panneels V., Sikorski M., Song S., Stahlberg H., Vartiainen I., Vera L., Wang M., Willmott P. R., David C. Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals. Struct. Dyn. 5 054303 (2018).
93. Huang C.-Y., Olieric V., Howe N., Warshamanage R., Weinert T., Panepucci E., Vogeley L., Basu S., Diederichs K., Caffrey M., Wang M.* In situ serial crystallography for rapid de novo membrane protein structure determination. Commun. Biol. 1, 124 (2018).
92. Gao X., Mu Z., Yu X., Qin B., Wojdyla J. A., Wang M., Cui S. Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase From Shigella flexneri. Front. Microbiol. 9, 1468 (2018).
91. Wang W., Qin B., Wojdyla J. A., Wang M., Gao X., Cui S. Structural characterization of free-state and product-state Mycobacterium tuberculosis methionyl-tRNA synthetase reveals an induced-fit ligand-recognition mechanism. IUCrJ 5, 478 (2018).
90. El Ghachi, M., Howe, N., Huang, C.-Y., Olieric, V., Warshamanage, R., Touzé, T., Weichert, D., Stansfeld, P. J., Wang, M., Kerff, F. & Caffrey, M. Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nat. Commun. 9, 1078 (2018).
89. Yin, W., Zhou, X. E., Yang, D., de Waal, P. W., Wang, M., Dai, A., Cai, X., Huang, C.-Y., Liu, P., Wang, X., Yin, Y., Liu, B., Zhou, Y., Wang, J., Liu, H., Caffrey, M., Melcher, K., Xu, Y., Wang, M.-W., Xu, H. E. & Jiang, Y. Crystal structure of the human 5-HT1Bserotonin receptor bound to an inverse agonist. Cell Discov 4, 12 (2018).
88. Wojdyla, J. A., Kaminski, J. W., Panepucci, E., Ebner, S., Wang, X., Gabadinho, J. & Wang, M.* DA+ data acquisition and analysis software at the Swiss Light Source macromolecular crystallography beamlines. J. Synchrotron Radiat. 25, 293–303 (2018).
87. Martiel, I., Olieric, V., Caffrey, M. & Wang, M.* Practical Approaches for In Situ X-ray Crystallography: from High-throughput Screening to Serial Data Collection. in Protein Crystallography 1–27 (2018).
86. Weinert, T., Olieric, N., Cheng, R., Brünle, S., James, D., Ozerov, D., Gashi, D., Vera, L., Marsh, M., Jaeger, K., Dworkowski, F., Panepucci, E., Basu, S., Skopintsev, P., Doré, A. S., Geng, T., Cooke, R. M., Liang, M., Prota, A. E., Panneels, V., Nogly, P., Ermler, U., Schertler, G., Hennig, M., Steinmetz, M. O., Wang, M. & Standfuss, J. Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nat. Commun. 8, 542 (2017).
85. Milne, C. J., Schietinger, T., Aiba, M., Alarcon, A., Alex, J., Anghel, A., Arsov, V., Beard, C., Beaud, P., Bettoni, S., Bopp, M., Brands, H., Brönnimann, M., Brunnenkant, I., Calvi, M., Citterio, A., Craievich, P., Csatari Divall, M., Dällenbach, M., D’Amico, M., Dax, A., Deng, Y., Dietrich, A., Dinapoli, R., Divall, E., Dordevic, S., Ebner, S., Erny, C., Fitze, H., Flechsig, U., Follath, R., Frei, F., Gärtner, F., Ganter, R., Garvey, T., Geng, Z., Gorgisyan, I., Gough, C., Hauff, A., Hauri, C. P., Hiller, N., Humar, T., Hunziker, S., Ingold, G., Ischebeck, R., Janousch, M., Juranić, P., Jurcevic, M., Kaiser, M., Kalantari, B., Kalt, R., Keil, B., Kittel, C., Knopp, G., Koprek, W., Lemke, H. T., Lippuner, T., Llorente Sancho, D., Löhl, F., Lopez-Cuenca, C., Märki, F., Marcellini, F., Marinkovic, G., Martiel, I., Menzel, R., Mozzanica, A., Nass, K., Orlandi, G. L., Ozkan Loch, C., Panepucci, E., Paraliev, M., Patterson, B., Pedrini, B., Pedrozzi, M., Pollet, P., Pradervand, C., Prat, E., Radi, P., Raguin, J.-Y., Redford, S., Rehanek, J., Réhault, J., Reiche, S., Ringele, M., Rittmann, J., Rivkin, L., Romann, A., Ruat, M., Ruder, C., Sala, L., Schebacher, L., Schilcher, T., Schlott, V., Schmidt, T., Schmitt, B., Shi, X., Stadler, M., Stingelin, L., Sturzenegger, W., Szlachetko, J., Thattil, D., Treyer, D. M., Trisorio, A., Tron, W., Vetter, S., Vicario, C., Voulot, D., Wang, M., Zamofing, T., Zellweger, C., Zennaro, R., Zimoch, E., Abela, R., Patthey, L. & Braun, H.-H. SwissFEL: The Swiss X-ray Free Electron Laser. NATO Adv. Sci. Inst. Ser. E Appl. Sci. 7, 720 (2017).
84. Wiktor, M., Weichert, D., Howe, N., Huang, C.-Y., Olieric, V., Boland, C., Bailey, J., Vogeley, L., Stansfeld, P. J., Buddelmeijer, N., Wang, M. & Caffrey, M. Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Nat. Commun. 8, 15952 (2017).
83. Hao, W., Wojdyla, J. A., Zhao, R., Han, R., Das, R., Zlatev, I., Manoharan, M., Wang, M. & Cui, S. Crystal structure of Middle East respiratory syndrome coronavirus helicase. PLoS Pathog. 13, e1006474 (2017).
82. Ou, X., Guan, H., Qin, B., Mu, Z., Wojdyla, J. A., Wang, M., Dominguez, S. R., Qian, Z. & Cui, S. Crystal structure of the receptor binding domain of the spike glycoprotein of human betacoronavirus HKU1. Nat. Commun. 8, 15216 (2017).
81. Guan, H., Tian, J., Qin, B., Wojdyla, J. A., Wang, B., Zhao, Z., Wang, M. & Cui, S. Crystal structure of 2C helicase from enterovirus 71. Sci Adv 3, e1602573 (2017).
80. Nöll, A., Thomas, C., Herbring, V., Zollmann, T., Barth, K., Mehdipour, A. R., Tomasiak, T. M., Brüchert, S., Joseph, B., Abele, R., Oliéric, V., Wang, M., Diederichs, K., Hummer, G., Stroud, R. M., Pos, K. M. & Tampé, R. Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP. Proc. Natl. Acad. Sci. U. S. A. 114, E438–E447 (2017).
79. Diederichs, K. & Wang, M. Serial Synchrotron X-Ray Crystallography (SSX). Methods Mol. Biol. 1607, 239–272 (2017).
78. Casanas, A., Warshamanage, R., Finke, A. D., Panepucci, E., Olieric, V., Nöll, A., Tampé, R., Brandstetter, S., Förster, A., Mueller, M., Schulze-Briese, C., Bunk, O. & Wang, M.* EIGER detector: application in macromolecular crystallography. Acta Crystallogr D Struct Biol 72, 1036–1048 (2016).
77. Tong, S., Lin, Y., Lu, S., Wang, M., Bogdanov, M. & Zheng, L. Structural Insight into Substrate Selection and Catalysis of Lipid Phosphate Phosphatase PgpB in the Cell Membrane. J. Biol. Chem. 291, 18342–18352 (2016).
76. Li, Y.-Y., Liu, P.-F., Lin, H., Wang, M. & Chen, L. The effect of indium substitution on the structure and NLO properties of Ba6Cs2Ga10Se20Cl4. Inorg. Chem. Front. 3, 952–958 (2016).
75. Schaffer, M. F., Peng, G., Spingler, B., Schnabl, J., Wang, M., Olieric, V. & Sigel, R. K. O. The X-ray Structures of Six Octameric RNA Duplexes in the Presence of Different Di- and Trivalent Cations. Int. J. Mol. Sci. 17, (2016).
74. Wojdyla, J. A., Panepucci, E., Martiel, I., Ebner, S., Huang, C.-Y., Caffrey, M., Bunk, O. & Wang, M.* Fast two-dimensional grid and transmission X-ray microscopy scanning methods for visualizing and characterizing protein crystals. J. Appl. Crystallogr. 49, 944–952 (2016).
73. Zhou, X. E., Gao, X., Barty, A., Kang, Y., He, Y., Liu, W., Ishchenko, A., White, T. A., Yefanov, O., Han, G. W., Xu, Q., de Waal, P. W., Suino-Powell, K. M., Boutet, S., Williams, G. J., Wang, M., Li, D., Caffrey, M., Chapman, H. N., Spence, J. C. H., Fromme, P., Weierstall, U., Stevens, R. C., Cherezov, V., Melcher, K. & Xu, H. E. X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. Sci Data 3, 160021 (2016).
72. Olieric, V., Weinert, T., Finke, A. D., Anders, C., Li, D., Olieric, N., Borca, C. N., Steinmetz, M. O., Caffrey, M., Jinek, M. & Wang, M. Data-collection strategy for challenging native SAD phasing. Acta Crystallogr D Struct Biol 72, 421–429 (2016).
71. Huang, C. Y., Olieric, V., Ma, P., Howe, N., Vogeley, L., Liu, X., Warshamanage, R., Weinert, T., Panepucci, E., Kobilka, B., Diederichs, K., Wang, M.* & Caffrey, M.* In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures. Acta Crystallogr D Struct Biol 72, 93–112 (2016).
70. Finke, A. D., Panepucci, E., Vonrhein, C., Wang, M., Bricogne, G. & Oliéric, V. Advanced Crystallographic Data Collection Protocols for Experimental Phasing. Methods Mol. Biol. 1320, 175–191 (2016).
69. Jaeger, K., Dworkowski, F., Nogly, P., Milne, C., Wang, M. & Standfuss, J. Serial Millisecond Crystallography of Membrane Proteins. Adv. Exp. Med. Biol. 922, 137–149 (2016).
68. Kang, Y., Zhou, X. E., Gao, X., He, Y., Liu, W., Ishchenko, A., Barty, A., White, T. A., Yefanov, O., Han, G. W., Xu, Q., de Waal, P. W., Ke, J., Tan, M. H. E., Zhang, C., Moeller, A., West, G. M., Pascal, B. D., Van Eps, N., Caro, L. N., Vishnivetskiy, S. A., Lee, R. J., Suino-Powell, K. M., Gu, X., Pal, K., Ma, J., Zhi, X., Boutet, S., Williams, G. J., Messerschmidt, M., Gati, C., Zatsepin, N. A., Wang, D., James, D., Basu, S., Roy-Chowdhury, S., Conrad, C. E., Coe, J., Liu, H., Lisova, S., Kupitz, C., Grotjohann, I., Fromme, R., Jiang, Y., Tan, M., Yang, H., Li, J., Wang, M., Zheng, Z., Li, D., Howe, N., Zhao, Y., Standfuss, J., Diederichs, K., Dong, Y., Potter, C. S., Carragher, B., Caffrey, M., Jiang, H., Chapman, H. N., Spence, J. C. H., Fromme, P., Weierstall, U., Ernst, O. P., Katritch, V., Gurevich, V. V., Griffin, P. R., Hubbell, W. L., Stevens, R. C., Cherezov, V., Melcher, K. & Xu, H. E. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561–567 (2015).
67. Waltersperger, S., Olieric, V., Pradervand, C., Glettig, W., Salathe, M., Fuchs, M. R., Curtin, A., Wang, X., Ebner, S., Panepucci, E., Weinert, T., Schulze-Briese, C. & Wang, M.* PRIGo: a new multi-axis goniometer for macromolecular crystallography. J. Synchrotron Radiat. 22, 895–900 (2015).
66. Huang, C. Y., Olieric, V., Ma, P., Panepucci, E., Diederichs, K., Wang, M.* & Caffrey, M.* In meso in situ serial X-ray crystallography of soluble and membrane proteins. Acta Crystallogr. D Biol. Crystallogr. 71, 1238–1256 (2015).
65. Xia, L., Lin, H., Staniek, A., Panjikar, S., Ruppert, M., Hilgers, P., Williardt, J., Rajendran, C., Wang, M., Warzecha, H., Jäger, V. & Stöckigt, J. Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours. J. Enzyme Inhib. Med. Chem. 30, 472–478 (2015).
64. Zhu, H., Kerčmar, P., Wu, F., Rajendran, C., Sun, L., Wang, M. & Stöckigt, J. Using Strictosidine Synthase to Prepare Novel Alkaloids. Curr. Med. Chem. 22, 1880–1888 (2015).
63. Chang, S., Sun, D., Liang, H., Wang, J., Li, J., Guo, L., Wang, X., Guan, C., Boruah, B. M., Yuan, L., Feng, F., Yang, M., Wang, L., Wang, Y., Wojdyla, J., Li, L., Wang, J., Wang, M., Cheng, G., Wang, H.-W. & Liu, Y. Cryo-EM structure of influenza virus RNA polymerase complex at 4.3 Å resolution. Mol. Cell 57, 925–935 (2015).
62. Botha, S., Nass, K., Barends, T. R. M., Kabsch, W., Latz, B., Dworkowski, F., Foucar, L., Panepucci, E., Wang, M., Shoeman, R. L., Schlichting, I. & Doak, R. B. Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams. Acta Crystallogr. D Biol. Crystallogr. 71, 387–397 (2015).
61. Weinert, T., Olieric, V., Waltersperger, S., Panepucci, E., Chen, L., Zhang, H., Zhou, D., Rose, J., Ebihara, A., Kuramitsu, S., Li, D., Howe, N., Schnapp, G., Pautsch, A., Bargsten, K., Prota, A. E., Surana, P., Kottur, J., Nair, D. T., Basilico, F., Cecatiello, V., Pasqualato, S., Boland, A., Weichenrieder, O., Wang, B.-C., Steinmetz, M. O., Caffrey, M. & Wang, M.* Fast native-SAD phasing for routine macromolecular structure determination. Nat. Methods 12, 131–133 (2015).
60. Chong, H., Yao, X., Qiu, Z., Sun, J., Qiao, Y., Zhang, M., Wang, M., Cui, S. & He, Y. The M-T hook structure increases the potency of HIV-1 fusion inhibitor sifuvirtide and overcomes drug resistance. J. Antimicrob. Chemother. 69, 2759–2769 (2014).
59. Li, D., Howe, N., Dukkipati, A., Shah, S. T. A., Bax, B. D., Edge, C., Bridges, A., Hardwicke, P., Singh, O. M. P., Giblin, G., Pautsch, A., Pfau, R., Schnapp, G., Wang, M., Olieric, V. & Caffrey, M. Crystallizing Membrane Proteins in the Lipidic Mesophase. Experience with Human Prostaglandin E2 Synthase 1 and an Evolving Strategy. Cryst. Growth Des. 14, 2034–2047 (2014).
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17. Morgan, M. G., Wang, M., Chan, W. Y. & Mar, A. Lanthanum gallium bismuthide, LaGaBi2. Inorg. Chem. 42, 1549–1555 (2003).
16. Ristic-Petrovic, D., Wang, M., McDonald, R. & Cowie, M. Binuclear Fluorovinyl Complexes of Iridium: Transformation of an Iridium-Bound Trifluorovinyl Group into a trans-[Ir−C(F)C(F)CH3] Moiety. Organometallics 21, 5172–5181 (2002).
15. Morgan, M. G., Wang, M. & Mar, A. Samarium orthosilicate oxyapatite, Sm5(SiO4)3O. Acta Crystallogr. Sect. E Struct. Rep. Online 58, i70–i71 (2002).
14. Morgan, M. G., Wang, M., Mills, A. M. & Mar, A. Lanthanum Gallium Tin Antimonides LaGaxSnySb2. J. Solid State Chem. 167, 41–47 (2002).
13. Lewis, C. A., Wang, M. & Mar, A. Vanadium nickel antimonide, VNi0.26(2) Sb. Acta Crystallogr. Sect. E Struct. Rep. Online 58, i39–i40 (2002).
12. Wang, M. & Mar, A. Nb9PdAs7: A Unique Arrangement in the Mn2+3n+2Xn2+nY Family of Hexagonal Structures. Inorg. Chem. 40, 5365–5370 (2001).
11. Wang, M. & Mar, A. Nb28Ni33.5Sb12.5, a New Representative of the X-phase. J. Solid State Chem. 160, 450–459 (2001).
10. Wang, M., Sheets, W. C., McDonald, R. & Mar, A. Nb4Pd0.5ZSb2 (Z = Cr, Fe, Co, Ni, Si): The First Ordered Quaternary Variants of the W5Si3-Type Structure. Inorg. Chem. 40, 5199–5205 (2001).
9. Norsten, T. B., Peters, A., McDonald, R., Wang, M. & Branda, N. R. Reversible [7]-Thiahelicene Formation Using a 1,2-Dithienylcyclopentene Photochrome. J. Am. Chem. Soc. 123, 7447–7448 (2001).
8. Wang, M., McDonald, R. & Mar, A. Ternary Early-Transition-Metal Palladium Pnictides Zr3Pd4P3, Hf3Pd4P3, HfPdSb, and Nb5Pd4P4. Inorg. Chem. 39, 4936–4941 (2000).
7. Wang, M. & Mar, A. High-temperature LaAs2. Acta Crystallogr. C 56 (Pt 2), 138–139 (2000).
6. Wang, M. & Mar, A. The Ternary Silicide ZrPd3Si3, a Stacking Variant of the α-FeSi2 and Re3B Structure Types. Chem. Mater. 11, 3232–3237 (1999).
5. Wang, M., McDonald, R. & Mar, A. Nonstoichiometric Rare-Earth Copper Arsenides RECu1+xAs2 (RE=La, Ce, Pr). J. Solid State Chem. 147, 140–145 (1999).
4. Wang, M., McDonald, R. & Mar, A. M(3)Ni(3)Sb(4) (M = Zr, Hf) and Zr(3)Pt(3)Sb(4). Ternary Antimonides with the Y(3)Au(3)Sb(4) Structure. Inorg. Chem. 38, 3435–3438 (1999).
3. Wang, M. & Mar, A. The ternary suicide ZrPd3Si3, a stacking variant of the α-FeSi2 and Re3B structure types. Chem. Mater. 11, 3232–3237 (1999).
2. Sun, Y., Wang, S., Qiao, Z. & Wang, M. Phase Diagram of EuI2–KI Binary System. J. Solid State Chem. 136, 134–136 (1998).
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Memberships
2018 Member of European Synchrotron Radiation Facility (ESRF) Science Advisory Committee
2018 Member of ESRF Beam Time Allocation Panel
2019 CHESS Beamtime Review Panel