Dr. Meitian Wang

photo of Meitian Wang

Head of MX and Group Leader (i.p.) MX Applications

Paul Scherrer Institute
Forschungsstrasse 111
5232 Villigen PSI
Switzerland



2010 Group leader, Swiss Light Source, Villigen-PSI, Switzerland

2006 Beamline scientist, Swiss Light Source, Villigen-PSI, Switzerland

2001 Ph.D. University of Alberta, Edmonton, Canada

Macromolecular crystallography beamline development

We use a science-driven and instrumentation-inspired approach in beamline development. We exploited two-stage dynamic focusing to fully control size and divergence of X-rays, implemented multi-axis goniometers to improve data accuracy, and developed single-photon counting detectors to record diffraction with the highest precision. Collectively, three SLS MX beamlines have delivered 5500 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 Biol72, 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).

Native-SAD phasing

We developed a low-dose multi-orientation data collection strategy for native-SAD phasing in 2014. 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.

a. Weinert, T. et al. Fast native-SAD phasing for routine macromolecular structure determination. Nat. Methods12, 131–133 (2015).

b. Olieric, V. et al. Data-collection strategy for challenging native SAD phasing. Acta Crystallogr D Struct Biol72, 421–429 (2016).

c. Finke, A. D. et al. Advanced Crystallographic Data Collection Protocols for Experimental Phasing. Methods Mol. Biol.1320, 175–191 (2016).

In mese in situ serial 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 valuable crystals. Together with Martin Caffrey at Trinity College Dublin, we developed in meso in situ serial crystallography (IMISX). IMISX enables in situ X-ray data collection with crystals in their growth environment in a serial manner and has been applied successfully to a broad range of membrane proteins.

a. Huang, C. Y. et al. In meso in situ serial X-ray crystallography of soluble and membrane proteins. Acta Crystallogr. D Biol. Crystallogr71, 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 Biol72, 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).

Serial synchrotron crystallography (SSX) with injectors

We have demonstrated that room-temperature structures can be determined from microcrystals in a serial crystallography approach by a combined use of LCP injector, micro-focused X-ray beam and fast frame-rate detectors (PILATUS and EIGER). The injector-based SSX enables room-temperature structure determination and dynamics study.

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).
The complete publication list: https://paperpile.com/shared/KT3I95

* corresponding author

89. 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).

88. 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).

87. 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).

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).

58. Fuchs, M. R., Pradervand, C., Thominet, V., Schneider, R., Panepucci, E., Grunder, M., Gabadinho, J., Dworkowski, F. S. N., Tomizaki, T., Schneider, J., Mayer, A., Curtin, A., Olieric, V., Frommherz, U., Kotrle, G., Welte, J., Wang, X., Maag, S., Schulze-Briese, C. & Wang, M. D3, the new diffractometer for the macromolecular crystallography beamlines of the Swiss Light Source. J. Synchrotron Radiat. 21, 340–351 (2014).

57. Gao, X., Zou, T., Mu, Z., Qin, B., Yang, J., Waltersperger, S., Wang, M., Cui, S. & Jin, Q. Structural insights into VirB-DNA complexes reveal mechanism of transcriptional activation of virulence genes. Nucleic Acids Res. 41, 10529–10541 (2013).

56. Feng, S., Chen, Y., Kamada, K., Wang, H., Tang, K., Wang, M. & Gao, Y.-G. YoeB-ribosome structure: a canonical RNase that requires the ribosome for its specific activity. Nucleic Acids Res. 41, 9549–9556 (2013).

55. Wu, M., Tong, S., Waltersperger, S., Diederichs, K., Wang, M. & Zheng, L. Crystal structure of Ca2+/H+ antiporter protein YfkE reveals the mechanisms of Ca2+ efflux and its pH regulation. Proc. Natl. Acad. Sci. U. S. A. 110, 11367–11372 (2013).

54. Xia, L., Rajendran, C., Ruppert, M., Panjikar, S., Wang, M. & Stoeckigt, J. High speed X-ray analysis of plant enzymes at room temperature. Phytochemistry 91, 88–92 (2013).

53. Chong, H., Yao, X., Qiu, Z., Sun, J., Zhang, M., Waltersperger, S., Wang, M., Liu, S.-L., Cui, S. & He, Y. Short-peptide fusion inhibitors with high potency against wild-type and enfuvirtide-resistant HIV-1. FASEB J. 27, 1203–1213 (2013).

52. Ran, T., Gao, Y., Marsh, M., Zhu, W., Wang, M., Mao, X., Xu, L., Xu, D. & Wang, W. Crystal structures of Cg1458 reveal a catalytic lid domain and a common catalytic mechanism for the FAH family. Biochem. J 449, 51–60 (2013).

51. Chong, H., Yao, X., Sun, J., Qiu, Z., Zhang, M., Waltersperger, S., Wang, M., Cui, S. & He, Y. The M-T hook structure is critical for design of HIV-1 fusion inhibitors. J. Biol. Chem. 287, 34558–34568 (2012).

50. Yao, X., Chong, H., Zhang, C., Qiu, Z., Qin, B., Han, R., Waltersperger, S., Wang, M., He, Y. & Cui, S. Structural basis of potent and broad HIV-1 fusion inhibitor CP32M. J. Biol. Chem. 287, 26618–26629 (2012).

49. Chong, H., Yao, X., Qiu, Z., Qin, B., Han, R., Waltersperger, S., Wang, M., Cui, S. & He, Y. Discovery of critical residues for viral entry and inhibition through structural Insight of HIV-1 fusion inhibitor CP621-652. J. Biol. Chem. 287, 20281–20289 (2012).

48. Zou, T., Yao, X., Qin, B., Zhang, M., Cai, L., Shang, W., Svergun, D. I., Wang, M., Cui, S. & Jin, Q. Crystal structure of Pseudomonas aeruginosa Tsi2 reveals a stably folded superhelical antitoxin. J. Mol. Biol. 417, 351–361 (2012).

47. Sun, L., Chen, Y., Rajendran, C., Mueller, U., Panjikar, S., Wang, M., Mindnich, R., Rosenthal, C., Penning, T. M. & Stöckigt, J. Crystal structure of perakine reductase, founding member of a novel aldo-keto reductase (AKR) subfamily that undergoes unique conformational changes during NADPH binding. J. Biol. Chem. 287, 11213–11221 (2012).

46. Wang, N., Wang, M., Gao, Y., Ran, T., Lan, Y., Wang, J., Xu, L. & Wang, W. Crystallization and preliminary X-ray crystallographic analysis of a blue-light-absorbing proteorhodopsin. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 281–283 (2012).

45. Yao, X., Chong, H., Zhang, C., Waltersperger, S., Wang, M., Cui, S. & He, Y. Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor sifuvirtide. J. Biol. Chem. 287, 6788–6796 (2012).

44. Wu, F., Zhu, H., Sun, L., Rajendran, C., Wang, M., Ren, X., Panjikar, S., Cherkasov, A., Zou, H. & Stöckigt, J. Scaffold tailoring by a newly detected Pictet-Spenglerase activity of strictosidine synthase: from the common tryptoline skeleton to the rare piperazino-indole framework. J. Am. Chem. Soc. 134, 1498–1500 (2012).

43. Xia, L., Ruppert, M., Wang, M., Panjikar, S., Lin, H., Rajendran, C., Barleben, L. & Stöckigt, J. Structures of alkaloid biosynthetic glucosidases decode substrate specificity. ACS Chem. Biol. 7, 226–234 (2012).

42. 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).

41. Wang, J., Fan, T., Yao, X., Wu, Z., Guo, L., Lei, X., Wang, J., Wang, M., Jin, Q. & Cui, S. Crystal structures of enterovirus 71 3C protease complexed with rupintrivir reveal the roles of catalytically important residues. J. Virol. 85, 10021–10030 (2011).

40. Cui, S.*, Wang, J., Fan, T., Qin, B., Guo, L., Lei, X., Wang, J., Wang, M.* & Jin, Q.* Crystal structure of human enterovirus 71 3C protease. J. Mol. Biol. 408, 449–461 (2011).

39. Rajendran, C., Dworkowski, F. S. N., Wang, M. & Schulze-Briese, C. Radiation damage in room-temperature data acquisition with the PILATUS 6M pixel detector. J. Synchrotron Radiat. 18, 318–328 (2011).

38. Bingel-Erlenmeyer, R., Olieric, V., Grimshaw, J. P. A., Gabadinho, J., Wang, X., Ebner, S. G., Isenegger, A., Schneider, R., Schneider, J., Glettig, W., Pradervand, C., Panepucci, E. H., Tomizaki, T., Wang, M. & Schulze-Briese, C. SLS Crystallization Platform at Beamline X06DA—A Fully Automated Pipeline Enabling in Situ X-ray Diffraction Screening. Cryst. Growth Des. 11, 916–923 (2011).

37. Waltersperger, S., Widmer, C., Wang, M. & Baumann, U. Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri at 1.5 A resolution. Proteins 78, 2720–2723 (2010).

36. Wu, M., Le, H. D., Wang, M., Yurkov, V., Omelchenko, A., Hnatowich, M., Nix, J., Hryshko, L. V. & Zheng, L. Crystal structures of progressive Ca2+ binding states of the Ca2+ sensor Ca2+ binding domain 1 (CBD1) from the CALX Na+/Ca2+ exchanger reveal incremental conformational transitions. J. Biol. Chem. 285, 2554–2561 (2010).

35. Wu, M., Wang, M., Nix, J., Hryshko, L. V. & Zheng, L. Crystal structure of CBD2 from the Drosophila Na(+)/Ca(2+) exchanger: diversity of Ca(2+) regulation and its alternative splicing modification. J. Mol. Biol. 387, 104–112 (2009).

34. Yang, L., Hill, M., Wang, M., Panjikar, S. & Stöckigt, J. Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids. Angew. Chem. Int. Ed Engl. 48, 5211–5213 (2009).

33. Varco-Merth, B., Fromme, R., Wang, M. & Fromme, P. Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments. Biochim. Biophys. Acta 1777, 605–612 (2008).

32. Malo, G. D., Wang, M., Wu, D., Stelling, A. L., Tonge, P. J. & Wachter, R. M. Crystal structure and Raman studies of dsFP483, a cyan fluorescent protein from Discosoma striata. J. Mol. Biol. 378, 871–886 (2008).

31. Malo, G. D., Pouwels, L. J., Wang, M., Weichsel, A., Montfort, W. R., Rizzo, M. A., Piston, D. W. & Wachter, R. M. X-ray structure of Cerulean GFP: a tryptophan-based chromophore useful for fluorescence lifetime imaging. Biochemistry 46, 9865–9873 (2007).

30. Smith, M. D., Rosenow, M. A., Wang, M., Allen, J. P., Szostak, J. W. & Chaput, J. C. Structural insights into the evolution of a non-biological protein: importance of surface residues in protein fold optimization. PLoS One 2, e467 (2007).

29. Cámara-Artigas, A., Hirasawa, M., Knaff, D. B., Wang, M. & Allen, J. P. Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62, 1087–1092 (2006).

28. Biswal, B. K., Wang, M., Cherney, M. M., Chan, L., Yannopoulos, C. G., Bilimoria, D., Bedard, J. & James, M. N. G. Non-nucleoside inhibitors binding to hepatitis C virus NS5B polymerase reveal a novel mechanism of inhibition. J. Mol. Biol. 361, 33–45 (2006).

27. Smith, A. W., Camara-Artigas, A., Wang, M., Allen, J. P. & Francisco, W. A. Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center. Biochemistry 45, 4378–4387 (2006).

26. Swamy, U., Wang, M., Tripathy, J. N., Kim, S.-K., Hirasawa, M., Knaff, D. B. & Allen, J. P. Structure of spinach nitrite reductase: implications for multi-electron reactions by the iron-sulfur:siroheme cofactor. Biochemistry 44, 16054–16063 (2005).

25. Lemieux, M. J., Ference, C., Cherney, M. M., Wang, M., Garen, C. & James, M. N. G. The crystal structure of Rv0793, a hypothetical monooxygenase from M. tuberculosis. J. Struct. Funct. Genomics 6, 245–257 (2005).

24. Biswal, B. K., Cherney, M. M., Wang, M., Garen, C. & James, M. N. G. Structures of Mycobacterium tuberculosispyridoxine 5’-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate. Acta Crystallogr. D Biol. Crystallogr. 61, 1492–1499 (2005).

23. Wang, M., Patel, H. N. & Wachter, R. M. X-ray diffraction analysis and molecular-replacement solution of the cyan fluorescent protein dsFP483. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61, 922–924 (2005).

22. Biswal, B. K., Cherney, M. M., Wang, M., Chan, L., Yannopoulos, C. G., Bilimoria, D., Nicolas, O., Bedard, J. & James, M. N. G. Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors. J. Biol. Chem. 280, 18202–18210 (2005).

21. Dennett, J. N. L., Jacke, J., Nilsson, G., Rosborough, A., Ferguson, M. J., Wang, M., McDonald, R. & Takats, J. Alkene Carbon−Hydrogen Bond Activation at a Heterobimetallic Center: [RuCo(CO)3(μ-CO)(η-C5Me5){μ-η2:η2-C(CF3)C(CF3)}]. Organometallics 23, 4478–4485 (2004).

20. Wang, M., Morgan, M. G. & Mar, A. Platinum silicon antimonide (PtSiSb). J. Solid State Chem. 175, 231–236 (2003).

19. Wang, M., Mar, A. & MacLean, E. J. Structure determination of niobium palladium arsenide, Nb5Pd4As4, from a 5×5×5μm3 crystal with synchrotron radiation. J. Solid State Chem. 172, 232–236 (2003).

18. Wang, M., Ng, K. K.-S., Cherney, M. M., Chan, L., Yannopoulos, C. G., Bedard, J., Morin, N., Nguyen-Ba, N., Alaoui-Ismaili, M. H., Bethell, R. C. & James, M. N. G. Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase. Crystal structures and mechanism of inhibition. J. Biol. Chem. 278, 9489–9495 (2003).

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).

1. Miller, G., Smith, M., Wang, M. & Wang, S. The synthesis and crystal structure of Rb4TmI6: Lattice energy calculations on networks of condensed cubes. J. Alloys Compd. 265, 140–145 (1998).
2018 Member of European Synchrotron Radiation Facility (ESRF) Science Advisory Committee

2018 Member of ESRF Beam Time Allocation Panel