'Cool' crystals: macromolecular cryocrystallography and radiation damage.

Macromolecular crystals commonly suffer rapid radiation damage during room temperature X-ray data collection. Therefore, data are now routinely collected with the sample held at around 100K, significantly reducing secondary radiation damage, and usually resulting in higher resolution and better quality data. At synchrotron sources, the frequent observation of radiation damage even at cryotemperatures has prompted the development of exciting new experiments aimed at characterising and reducing this damage, and using it for structure determination and enzymatic studies. Current research into cryotechniques seeks to understand the basic physical and chemical processes involved in flash-cooling and radiation damage, which should eventually enable the rational optimisation of cryoprotocols.

[1]  S. Kriminski,et al.  Flash-cooling and annealing of protein crystals. , 2002, Acta crystallographica. Section D, Biological crystallography.

[2]  M. Murakami,et al.  Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin. , 2002, Journal of molecular biology.

[3]  M. Facciotti,et al.  Characterization of conditions required for X-Ray diffraction experiments with protein microcrystals. , 2000, Biophysical journal.

[4]  W. Burmeister,et al.  Structural changes in a cryo-cooled protein crystal owing to radiation damage. , 2000, Acta crystallographica. Section D, Biological crystallography.

[5]  E. Weckert,et al.  Investigation of radiation-dose-induced changes in organic light-atom crystals by accurate d-spacing measurements. , 2002, Journal of synchrotron radiation.

[6]  J. Hajdu,et al.  The catalytic pathway of horseradish peroxidase at high resolution , 2002, Nature.

[7]  B. Hanson,et al.  New techniques in macromolecular cryocrystallography: macromolecular crystal annealing and cryogenic helium. , 2003, Journal of structural biology.

[8]  T. Teng,et al.  Mounting of crystals for macromolecular crystallography in a free-standing thin film , 1990 .

[9]  A. Schmidt,et al.  Veni, vidi, vici - atomic resolution unravelling the mysteries of protein function. , 2002, Current opinion in structural biology.

[10]  Akinori Kidera,et al.  Nonlinear temperature dependence of the crystal structure of lysozyme: correlation between coordinate shifts and thermal factors. , 2002, Acta crystallographica. Section D, Biological crystallography.

[11]  C. Nave,et al.  Modelling heating effects in cryocooled protein crystals , 2001 .

[12]  S Kriminski,et al.  Heat transfer from protein crystals: implications for flash-cooling and X-ray beam heating. , 2003, Acta crystallographica. Section D, Biological crystallography.

[13]  J. Ferrer,et al.  X-ray-induced debromination of nucleic acids at the Br K absorption edge and implications for MAD phasing. , 2002, Acta crystallographica. Section D, Biological crystallography.

[14]  J. Sussman,et al.  Solvent behaviour in flash-cooled protein crystals at cryogenic temperatures. , 2001, Acta crystallographica. Section D, Biological crystallography.

[15]  J. Sussman,et al.  Specific protein dynamics near the solvent glass transition assayed by radiation‐induced structural changes , 2001, Protein science : a publication of the Protein Society.

[16]  M. Caffrey,et al.  Unit-cell volume change as a metric of radiation damage in crystals of macromolecules. , 2002, Journal of synchrotron radiation.

[17]  E Garman,et al.  Cool data: quantity AND quality. , 1999, Acta crystallographica. Section D, Biological crystallography.

[18]  K. Moffat,et al.  Radiation damage of protein crystals at cryogenic temperatures between 40 K and 150 K. , 2002, Journal of synchrotron radiation.

[19]  J L Sussman,et al.  Specific chemical and structural damage to proteins produced by synchrotron radiation. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[20]  Sean McSweeney,et al.  Zero-dose extrapolation as part of macromolecular synchrotron data reduction. , 2003, Acta crystallographica. Section D, Biological crystallography.

[21]  E. Snell,et al.  The development and application of a method to quantify the quality of cryoprotectant solutions using standard area-detector X-ray images , 2002 .

[22]  S. Harrison,et al.  How does radiation damage in protein crystals depend on X-ray dose? , 2003, Structure.

[23]  E. Garman,et al.  Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography. , 2002, Journal of synchrotron radiation.

[24]  B. J. Hsieh,et al.  X-ray beam/biomaterial thermal interactions in third-generation synchrotron sources. , 2001, Acta crystallographica. Section D, Biological crystallography.

[25]  R. Ravelli,et al.  The 'fingerprint' that X-rays can leave on structures. , 2000, Structure.

[26]  M. J. van der Woerd,et al.  Seeing the heat -- preliminary studies of cryocrystallography using infrared imaging. , 2002, Journal of synchrotron radiation.

[27]  B. Matthews,et al.  Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions. , 2001, Journal of molecular biology.

[28]  Richard Henderson,et al.  Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction , 1990, Proceedings of the Royal Society of London. Series B: Biological Sciences.

[29]  Sean McSweeney,et al.  Specific radiation damage can be used to solve macromolecular crystal structures. , 2003, Structure.

[30]  K. Moffat,et al.  Primary radiation damage of protein crystals by an intense synchrotron X-ray beam. , 2000, Journal of synchrotron radiation.