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Specific radiation damage is a lesser concern at room temperature.

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Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A
OpenAccess logo IUCrJ 6 665-680 (2019)
Related entries: 6qq8, 6qq9, 6qqa, 6qqc, 6qqd, 6qqe, 6qqf, 6qqh, 6qqi, 6qqj, 6qqk, 6qsa

Cited: 28 times
EuropePMC logo PMID: 31316810

Abstract

Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources.

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  1. Specific radiation damage is a lesser concern at room temperature. Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A. IUCrJ 6 665-680 (2019)


Reviews citing this publication (1)

  1. Best practices for time-resolved serial synchrotron crystallography. Schulz EC, Yorke BA, Pearson AR, Mehrabi P. Acta Crystallogr D Struct Biol 78 14-29 (2022)

Articles citing this publication (26)

  1. Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures. de la Mora E, Coquelle N, Bury CS, Rosenthal M, Holton JM, Carmichael I, Garman EF, Burghammer M, Colletier JP, Weik M. Proc Natl Acad Sci U S A 117 4142-4151 (2020)
  2. xia2.multiplex: a multi-crystal data-analysis pipeline. Gildea RJ, Beilsten-Edmands J, Axford D, Horrell S, Aller P, Sandy J, Sanchez-Weatherby J, Owen CD, Lukacik P, Strain-Damerell C, Owen RL, Walsh MA, Winter G. Acta Crystallogr D Struct Biol 78 752-769 (2022)
  3. Serial Femtosecond Zero Dose Crystallography Captures a Water-Free Distal Heme Site in a Dye-Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in FeIV =O Formation. Lučić M, Svistunenko DA, Wilson MT, Chaplin AK, Davy B, Ebrahim A, Axford D, Tosha T, Sugimoto H, Owada S, Dworkowski FSN, Tews I, Owen RL, Hough MA, Worrall JAR. Angew Chem Int Ed Engl 59 21656-21662 (2020)
  4. Instrumentation and experimental procedures for robust collection of X-ray diffraction data from protein crystals across physiological temperatures. Doukov T, Herschlag D, Yabukarski F. J Appl Crystallogr 53 1493-1501 (2020)
  5. Rapid and efficient room-temperature serial synchrotron crystallography using the CFEL TapeDrive. Zielinski KA, Prester A, Andaleeb H, Bui S, Yefanov O, Catapano L, Henkel A, Wiedorn MO, Lorbeer O, Crosas E, Meyer J, Mariani V, Domaracky M, White TA, Fleckenstein H, Sarrou I, Werner N, Betzel C, Rohde H, Aepfelbacher M, Chapman HN, Perbandt M, Steiner RA, Oberthuer D. IUCrJ 9 778-791 (2022)
  6. A shared vision for macromolecular crystallography over the next five years. Förster A, Schulze-Briese C. Struct Dyn 6 064302 (2019)
  7. Directionality of light absorption and emission in representative fluorescent proteins. Myšková J, Rybakova O, Brynda J, Khoroshyy P, Bondar A, Lazar J. Proc Natl Acad Sci U S A 117 32395-32401 (2020)
  8. Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography. Huang CY, Aumonier S, Engilberge S, Eris D, Smith KML, Leonarski F, Wojdyla JA, Beale JH, Buntschu D, Pauluhn A, Sharpe ME, Metz A, Olieric V, Wang M. Acta Crystallogr D Struct Biol 78 964-974 (2022)
  9. Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals. Yabukarski F, Doukov T, Mokhtari DA, Du S, Herschlag D. Acta Crystallogr D Struct Biol 78 945-963 (2022)
  10. Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron. Aumonier S, Santoni G, Santoni G, Gotthard G, von Stetten D, Leonard GA, Royant A. IUCrJ 7 728-736 (2020)
  11. Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization. Thorne RE. Acta Crystallogr D Struct Biol 79 78-94 (2023)
  12. Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi. Mikolajek H, Sanchez-Weatherby J, Sandy J, Gildea RJ, Campeotto I, Cheruvara H, Clarke JD, Foster T, Fujii S, Paulsen IT, Shah BS, Hough MA. IUCrJ 10 420-429 (2023)
  13. editorial Radiation damage to biological samples: still a pertinent issue. Garman EF, Weik M. J Synchrotron Radiat 28 1278-1283 (2021)
  14. Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature. Aumonier S, Engilberge S, Caramello N, von Stetten D, Gotthard G, Leonard GA, Mueller-Dieckmann C, Royant A. IUCrJ 9 756-767 (2022)
  15. A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography. Ghosh S, Zorić D, Dahl P, Bjelčić M, Johannesson J, Sandelin E, Borjesson P, Björling A, Banacore A, Edlund P, Aurelius O, Milas M, Nan J, Shilova A, Gonzalez A, Mueller U, Brändén G, Neutze R. J Appl Crystallogr 56 449-460 (2023)
  16. Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature. Moreno-Chicano T, Carey LM, Axford D, Beale JH, Doak RB, Duyvesteyn HME, Ebrahim A, Henning RW, Monteiro DCF, Myles DA, Owada S, Sherrell DA, Straw ML, Šrajer V, Sugimoto H, Tono K, Tosha T, Tews I, Trebbin M, Strange RW, Weiss KL, Worrall JAR, Meilleur F, Owen RL, Ghiladi RA, Hough MA. IUCrJ 9 610-624 (2022)
  17. Megahertz pulse trains enable multi-hit serial femtosecond crystallography experiments at X-ray free electron lasers. Holmes S, Kirkwood HJ, Bean R, Giewekemeyer K, Martin AV, Hadian-Jazi M, Wiedorn MO, Oberthür D, Marman H, Adriano L, Al-Qudami N, Bajt S, Barák I, Bari S, Bielecki J, Brockhauser S, Coleman MA, Cruz-Mazo F, Danilevski C, Dörner K, Gañán-Calvo AM, Graceffa R, Fanghor H, Heymann M, Frank M, Kaukher A, Kim Y, Kobe B, Knoška J, Laurus T, Letrun R, Maia L, Messerschmidt M, Metz M, Michelat T, Mills G, Molodtsov S, Monteiro DCF, Morgan AJ, Münnich A, Peña Murillo GE, Previtali G, Round A, Sato T, Schubert R, Schulz J, Shelby M, Seuring C, Sellberg JA, Sikorski M, Silenzi A, Stern S, Sztuk-Dambietz J, Szuba J, Trebbin M, Vagovic P, Ve T, Weinhausen B, Wrona K, Xavier PL, Xu C, Yefanov O, Nugent KA, Chapman HN, Mancuso AP, Barty A, Abbey B, Darmanin C. Nat Commun 13 4708 (2022)
  18. SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique. Stachowski TR, Snell ME, Snell EH. PLoS One 15 e0239702 (2020)
  19. From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons. Caramello N, Royant A. Acta Crystallogr D Struct Biol 80 60-79 (2024)
  20. Implementation of wedged-serial protein crystallography at PROXIMA-1. Chaussavoine I, Isabet T, Lener R, Montaville P, Vasireddi R, Chavas LMG. J Synchrotron Radiat 29 439-446 (2022)
  21. A SAXS-based approach to rationally evaluate radical scavengers - toward eliminating radiation damage in solution and crystallographic studies. Stachowski TR, Snell ME, Snell EH. J Synchrotron Radiat 28 1309-1320 (2021)
  22. Capturing the blue-light activated state of the Phot-LOV1 domain from Chlamydomonas reinhardtii using time-resolved serial synchrotron crystallography. Gotthard G, Mous S, Weinert T, Maia RNA, James D, Dworkowski F, Gashi D, Furrer A, Ozerov D, Panepucci E, Wang M, Schertler GFX, Heberle J, Standfuss J, Nogly P. IUCrJ 11 792-808 (2024)
  23. Evaluation of the data-collection strategy for room-temperature micro-crystallography studied by serial synchrotron rotation crystallography combined with the humid air and glue-coating method. Hasegawa K, Baba S, Kawamura T, Yamamoto M, Kumasaka T. Acta Crystallogr D Struct Biol 77 300-312 (2021)
  24. Microfluidic rotating-target device capable of three-degrees-of-freedom motion for efficient in situ serial synchrotron crystallography. Zhao FZ, Wang ZJ, Xiao QJ, Yu L, Sun B, Hou Q, Chen LL, Liang H, Wu H, Guo WH, He JH, Wang QS, Yin DC. J Synchrotron Radiat 30 347-358 (2023)
  25. Serial macromolecular crystallography at ALBA Synchrotron Light Source. Martin-Garcia JM, Botha S, Hu H, Jernigan R, Castellví A, Lisova S, Gil F, Calisto B, Crespo I, Roy-Chowdhury S, Grieco A, Ketawala G, Weierstall U, Spence J, Fromme P, Zatsepin N, Boer DR, Carpena X. J Synchrotron Radiat 29 896-907 (2022)
  26. Identifying and avoiding radiation damage in macromolecular crystallography. Shelley KL, Garman EF. Acta Crystallogr D Struct Biol 80 314-327 (2024)


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