Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 3, 2010, Pages 1094-1099

  Meents, Alke ^a,b   Gutmann, Sascha ^a,d   Wagner, Armin ^c   Schulze Briese, Clemens ^a  

^a PAUL SCHERRER INSTITUTE   (Switzerland)

^b DESY   (Germany)

^c DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^d NOVARTIS PHARMA AG   (Switzerland)

Author keywords

Cryocrystallography; Hydrogen abstraction; Macromolecular crystallography; Small angle x ray scattering; X ray radiolysis

Indexed keywords

DISULFIDE; ELASTASE; HYDROGEN; INSULIN;

ARTICLE; ATOM; CHEMICAL STRUCTURE; CONTROLLED STUDY; ELECTRON; ELECTRON MICROSCOPY; IONIZING RADIATION; IRRADIATION; PRIORITY JOURNAL; RADIOLYSIS; SMALL ANGLE SCATTERING; TEMPERATURE DEPENDENCE; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

COLD TEMPERATURE; CRYSTALLOGRAPHY, X-RAY; X-RAYS;

EID: 75749092651     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0905481107     Document Type: Article

References (40)

1. Henderson R (1990) Cryo-protection of protein crystals against radiation damage in electron and x-ray diffraction. Proc Roy Soc Lond B Bio, 241:6-8.
2. Nave C (1995) Radiation damage in protein crystallography. Radiat Phys Chem, 45(3):483-490.
3. Teng T-y, Moffat K (2000) Primary radiation damage of protein crystals by an intense synchrotron x-ray beam. J Synchrotron Radiat, 7(5):313-317.
4. Mozumder A, Magee JL (1966) Model of tracks of ionizing radiations for radical reaction mechanisms. Radiat Res, 28(2):203-214.
5. Ziaja B, London RA, Hajdu J (2005) Unified model of secondary electron cascades in diamond. J Appl Phys, 97(6):064905-064909.
6. Magdoff BS (1953) Deterioration of the crystallinity of wet ribonucleasewith exposure to x-radiation. Acta Crystallogr, 6:801-802.
7. Blake CFF, Phillips DC (1962) Effects of X-irradiation on single crystals of myoglobin. Biological Effects of Ionizing Radiation at the Molecular Level, International Atomic Energy Agency Symposium International Atomic Energy Agency, Vienna pp 183-191.
8. Teng TY (1990) Mounting of crystals for macromolecular crystallography in a free-standing thin film. J Appl Crystallogr, 23(5):387-391.
9. Ravelli RB, Theveneau P, McSweeney S, Caffrey M (2002) Unit-cell volume change as a metric of radiation damage in crystals of macromolecules. J Synchrotron Radiat, 9(6):355-360.
10. Burmeister W (2000) Structural changes in a cryo-cooled protein crystal owing to radiation damage. Acta Crystallogr D, 56(3):328-341.
11. Ravelli RB, McSweeney SM (2000) The "fingerprint" that x-rays can leave on structures. Structure, 8(3):315-328.
12. Weik M, et al. (2001) Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes. Protein Sci, 10(10):1953-1961.
13. Muller R, Weckert E, Zellner J, Drakopoulos M (2002) Investigation of radiation-dose-induced changes in organic light-atom crystals by accurate d-spacing measurements. J Synchrotron Radiat, 9(6):368-374.
14. Weik M, et al. (2000) Specific chemical and structural damage to proteins produced by synchrotron radiation. Proc Natl Acad Sci USA, 97(2):623-628.
15. Hope H (1988) Cryocrystallography of biological macromolecules: A generally applicable method. Acta Crystallogr B, 44(1):22-26.
16. Young ACM, Dewan JC, Thompson AW, Nave C (1990) Enhancement in resolution and lack of radiation damage in a rapidly frozen lysozyme crystal subjected to high-intensity synchrotron radiation. J Appl Crystallogr, 23(3):215-218.
17. Garman EF, Schneider TR (1997) Macromolecular cryocrystallography. J Appl Crystallogr, 30(3):211-237.
18. McDowall AW, et al. (1983) Electron microscopy of frozen hydrated sections of vitreous ice and vitrified biological samples. J Microsc, 131(1):1-9.
19. Dubochet J, Booy FP, Freeman R, Jones AV, Walter CA (1981) Low temperature electron microscopy. Annu Rev Biophys Bioeng, 10:133-149.
20. Knapek E, Dubochet J (1980) Beam damage to organic material is considerably reduced in cryo-electron microscopy. J Mol Biol, 141(2):147-161.
21. Chiu WDK, , Dubochet J, Glaeser RM, Heide HGet al. (1986) Cryoprotection in electron microscopy. J Microsc, 141:385-391.
22. Iancu CV, Wright ER, Heymann JB, Jensen GJ (2006) A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography. J Struct Biol, 153(3):231-240.
23. Chinte U, et al. (2007) Cryogenic (<20 K) helium coolingmitigates radiation damage to protein crystals. Acta Crystallogr D, 63(4):486-492.
24. Meents A, et al. (2007) Reduction of x-ray-induced radiation damage of macromolecular crystals by data collection at 15 K: A systematic study. Acta Crystallogr, 63(3):302-309.
25. Grabolle M, Haumann M, Muller C, Liebisch P, Dau H (2006) Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by x-ray irradiation at 10-300 K. J Biol Chem, 281(8):4580-4588.
26. Yano J, et al. (2005) X-ray damage to the Mn4Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography. Proc Natl Acad Sci USA, 102(34):12047-12052.
27. Corbett MC, et al. (2007) Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation. Acta Crystallogr D, 63(9):951-960.
28. Owen RL, Rudino-Pinera E, Garman EF (2006) Experimental determination of the radiation dose limit for cryocooled protein crystals. Proc Natl Acad Sci USA, 103(13):4912-4917.
29. Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I (2007) Cryoradiolytic reduction of crystalline heme proteins: Analysis by UV-Vis spectroscopy and x-ray crystallography. J Synchrotron Radiat, 14(1):11-23.
30. Murray J, Garman E (2002) Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography. J Synchrotron Radiat, 9(6):347-354.
31. Dubochet J (1988) Cryo-electron microscopy of vitrified specimens. Q Rev Biophys, 21(2):129-228.
32. Leapman RD, Sun S (1995) Cryo-electron energy loss spectroscopy: Observations on vitrified hydrated specimens and radiation damage. Ultramicroscopy, 59(1-4):71-79.
33. Symons MCR (1982) Radiation processes in frozen aqueous systems. Ultramicroscopy, 10(1-2):97-103.
34. Cook RJ, Whiffen DH (1962) Electron spin resonance and its application. Phys Med Biol, 7:277-300.
35. Mao WL, et al. (2002) Hydrogen clusters in clathrate hydrate. Science, 297(5590): 2247-2249.
36. Schulze-Briese C, Wagner A, Tomizaki T, Oetiker M (2005) Beam-size effects in radiation damage in insulin and thaumatin crystals. J Synchrotron Radiat, 12(3):261-267.
37. Broennimann C, et al. (2006) The PILATUS 1M detector. J Synchrotron Radiat, 13(2):120-130.
38. Kabsch W (2001) Crystallography of Biological Macromolecules. International Tables for Crystallography, (Kluwer, Dordrecht, The Netherlands), Vol F.
39. Murray JW, Garman EF, Ravelli RBG (2004) X-ray absorption by macromolecular crystals: The effects of wavelength and crystal composition on absorbed dose. J Appl Crystallogr, 37(4):513-522.
40. Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D, 58(11):1948-1954.