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BL02U1: the relocated macromolecular crystallography beamline at the Shanghai Synchrotron Radiation Facility

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Abstract

Macromolecular crystallography beamline BL17U1 at the Shanghai Synchrotron Radiation Facility has been relocated, upgraded, and given a new ID (BL02U1). It now delivers X-rays in the energy range of 6–16 keV, with a focused beam of 11.6 µm × 4.8 µm and photon flux greater than 1012 phs/s. The high credibility and stability of the beam and good timing synchronization of the equipment significantly improve the experimental efficiency. Since June 2021, when it officially opened to users, over 4200 h of beamtime have been provided to over 200 research groups to collect data at the beamline. Its good performance and stable operation have led to the resolution of several structures based on data collected at the beamline.

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Data availability statement

The data that support the findings of this study are openly available in Science Data Bank at https://www.doi.org/10.57760/sciencedb.j00186.00322 and https://cstr.cn/31253.11.sciencedb.j00186.00322.

References

  1. Q.S. Wang, F. Yu, S. Huang et al., The macromolecular crystallography beamline of SSRF. Nucl. Sci. Tech. 26, 010102 (2015). https://doi.org/10.13538/j.1001-8042/nst.26.010102

  2. D. Deng, C. Yan, X. Pan et al., Structural basis for sequence-specific recognition of DNA by TAL effectors. Science 335, 720–723 (2012). https://doi.org/10.1126/science.1215670

    Article  ADS  Google Scholar 

  3. D. Deng, C. Xu, P. Sun et al., Crystal structure of the human glucose transporter GLUT1. Nature 510, 121–125 (2014). https://doi.org/10.1038/nature13306

    Article  ADS  Google Scholar 

  4. W. Wang, L.J. Yu, C. Xu et al., Structural basis for blue-green light harvesting and energy dissipation in diatoms. Science 363, eaav0365 (2019). https://doi.org/10.1126/science.aav0365

    Article  Google Scholar 

  5. Z. Jin, X. Du, Y. Xu et al., Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors. Nature 582, 289–293 (2020). https://doi.org/10.1038/s41586-020-2223-y

    Article  ADS  Google Scholar 

  6. Q. Wang, Y. Zhang, L. Wu et al., Structural and functional basis of SARS-CoV-2 entry by using human ACE2. Cell 181(4), 894–904.e9 (2020). https://doi.org/10.1016/j.cell.2020.03.045

    Article  Google Scholar 

  7. J. Lan, J. Ge, J. Yu et al., Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 581, 215–220 (2020). https://doi.org/10.1038/s41586-020-2180-5

    Article  ADS  Google Scholar 

  8. W. Dai, B. Zhang, X.M. Jiang et al., Structure-based design of antiviral drug candidates targeting the sars-cov-2 main protease. Science 368, 1331–1335 (2020). https://doi.org/10.1126/science.abb4489

    Article  ADS  Google Scholar 

  9. B. Ju, Q. Zhang, J. Ge et al., Human neutralizing antibodies elicited by SARS-CoV-2 infection. Nature 584, 115–119 (2020). https://doi.org/10.1038/s41586-020-2380-z

    Article  ADS  Google Scholar 

  10. R. Shi, C. Shan, X. Duan et al., A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2. Nature 584, 120–124 (2020). https://doi.org/10.1038/s41586-020-2381-y

    Article  ADS  Google Scholar 

  11. Y. Wu, F. Wang, C. Shen et al., A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2. Science 368, 1274–1278 (2020). https://doi.org/10.1126/science.abc2241

    Article  ADS  Google Scholar 

  12. L. Dai, T. Zheng, K. Xu et al., A universal design of betacoronavirus vaccines against COVID-19, MERS, and SARS. Cell 182(3), 722–733 (2020). https://doi.org/10.1016/j.cell.2020.06.035

    Article  Google Scholar 

  13. S. Du, Y. Cao, Q. Zhu et al., Structurally resolved SARS-CoV-2 antibody shows high efficacy in severely infected hamsters and provides a potent cocktail pairing strategy. Cell 183, 1013–1023 (2020). https://doi.org/10.1016/j.cell.2020.09.035

    Article  Google Scholar 

  14. https://ir.beigene.com/news/u-s-fda-grants-beigene-s-brukinsa-zanubrutinib-accelerated-approval-to-treat-adult-patients-with-mantle-cell/0b15b271-6756-4620-ab0a-d23061d679dd/

  15. A. Burkhardt, T. Pakendorf, B. Reime et al., Status of the crystallography beamlines at PETRA III. Eur. Phys. J. Plus 131, 56 (2016). https://doi.org/10.1140/epjp/i2016-16056-0

    Article  Google Scholar 

  16. J. Sanchez-Weatherby, J. Sandy, H. Mikolajek et al., VMXi: a fully automated, fully remote, high-flux in situ macromolecular crystallography beamline. J. Synchrotron Rad. 26, 291–301 (2019). https://doi.org/10.1107/S1600577518015114

    Article  Google Scholar 

  17. T. Ursby, K. Ahnberg, R. Appio et al., BioMAX – the first macromolecular crystallography beamline at MAX IV Laboratory. J. Synchrotron Rad. 27, 1415–1429 (2020). https://doi.org/10.1107/S1600577520008723

    Article  Google Scholar 

  18. D.K. Schneider, W. Shi, B. Andi et al., FMX – the frontier microfocusing macromolecular crystallography beamline at the national synchrotron light source II. J. Synchrotron Rad. 28, 650–665 (2021). https://doi.org/10.1107/S1600577520016173

    Article  Google Scholar 

  19. M. Nanao, S. Basu, U. Zander et al., ID23-2: an automated and high-performance microfocus beamline for macromolecular crystallography at the ESRF. J. Synchrotron Rad. 29, 581–590 (2022). https://doi.org/10.1107/S1600577522000984

    Article  Google Scholar 

  20. E.A. Stern, Y. Yacoby, G.T. Seidler et al., Reducing radiation damage in macromolecular crystals at synchrotron sources. Acta Cryst. D 65, 366–374 (2009). https://doi.org/10.1107/S090744490900540X

    Article  Google Scholar 

  21. R. Sanishvili, D.W. Yoder, S.B. Pothineni et al., Radiation damage in protein crystals is reduced with a micron-sized X-ray beam. PNAS 108, 6127–6132 (2011). https://doi.org/10.1073/pnas.1017701108

    Article  ADS  Google Scholar 

  22. R. Sanishvili, V. Nagarajan, D. Yoder et al., A 7 µm mini-beam improves diffraction data from small or imperfect crystals of macromolecules. Acta Cryst. D 64, 425–435 (2008). https://doi.org/10.1107/S0907444908001741

    Article  Google Scholar 

  23. Q.S. Wang, K.H. Zhang, Y. Cui et al., Upgrade of macro- molecular crystallography beamline BL17U1at SSRF. Nucl. Sci. Tech. 29, 68 (2018). https://doi.org/10.1007/s41365-018-0398-9

    Article  Google Scholar 

  24. .Y. Zhong, Q.S. Wang, K. Liu et al. Optimized focusing plan for short X-ray wavelengths mode at BL17U in SSRF. Nuclear Techniques 41(5), 050102 (2018) (in Chinese) https://doi.org/10.11889/j.0253-3219.2018.hjs.41.050102https://doi.org/10.11889/j.0253-3219.2018.hjs.41.050102

  25. Z. Hu, C. Hong, W. Hua et al., Online monitoring of hard X-Ray beam at SSRF. Acta Optica Sin. 41(15), 1534001 (2021). https://doi.org/10.3788/AOS202141.1534001

    Article  Google Scholar 

  26. F. Yu, Q. Wang, M. Li et al., Aquarium: an automatic data-processing and experiment information management system for biological macromolecular crystallography beamlines. J. Appl. Cryst. 52, 472–477 (2019). https://doi.org/10.1107/S1600576719001183

    Article  ADS  Google Scholar 

  27. P. Han, L. Li, S. Liu et al., Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2. Cell 185(4), 630–640 (2022). https://doi.org/10.1016/j.cell.2022.01.001

    Article  Google Scholar 

  28. B. Wei, T. Zhang, P. Wang et al., Anti-infective therapy using species-specific activators of Staphylococcus aureus ClpP. Nat. Commun. 13, 6909 (2022). https://doi.org/10.1038/s41467-022-34753-0

    Article  ADS  Google Scholar 

  29. J. Deng, T.J. Wilson, J. Wang et al., Structure and mechanism of a methyltransferase ribozyme. Nat. Chem. Biol. 18, 556–564 (2022). https://doi.org/10.1038/s41589-022-00982-z

    Article  Google Scholar 

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Acknowledgements

We thank the staff of the department of beam engineering technology in SSRF for the engineering design and installation, as well as the financial support of the SSRF Phase-II project.

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Authors and Affiliations

Authors

Contributions

All authors contributed to the study conception and design. Feng Yu and Qi-Sheng Wang contributed to the general study conception, financial support, and supervision of this study. Ke Liu contributed to the beamline design. Feng Yu contributed to the experimental station design. Qin Xu and Wei-Wei Wang contributed to the material preparation. Huan Zhou and Hua-Ting Kong contributed to the data collection and formal data analysis. Kun-Hao Zhang and Qiang-Yan Pan contributed to the diffractometer design. Min-Jun Li, Zhi-Jun Wang and Xing-Ya Wang reviewed the manuscript and gave many useful suggestions. The first draft of the manuscript was written by Ke Liu and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.

Corresponding authors

Correspondence to Feng Yu or Qi-Sheng Wang.

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Conflict of interest

The authors declare that they have no competing interests.

Additional information

This work was supported by the National Key Research and Development Program of China (No. 2021YFC2301405), the National Natural Science Foundation of China (No. 31971121), and Shanghai Science and Technology Plan Project (No. 21ZR14718).

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Liu, K., Zhou, H., Xu, Q. et al. BL02U1: the relocated macromolecular crystallography beamline at the Shanghai Synchrotron Radiation Facility. NUCL SCI TECH 34, 193 (2023). https://doi.org/10.1007/s41365-023-01348-3

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