ArticleActa crystallographica. Section D, Biological crystallography2010
Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 66 citations in OpenAlex.
- Damage-limited resolution for X-ray and electron microscopy of organic specimens.Acta crystallographica. Section D, Structural biology · 2026Article
- A structural perspective on the temperature-dependent activity of enzymes.bioRxiv : the preprint server for biology · 2024Article
- Facing the phase problem.IUCrJ · 2023Article
- Polymer-based microfluidic device for on-chip counter-diffusive crystallization andLab on a chip · 2023Article
- Obtaining anomalous and ensemble information from protein crystals from 220 K up to physiological temperatures.Acta crystallographica. Section D, Structural biology · 2023Article
- Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.Acta crystallographica. Section D, Structural biology · 2023Article
- Refinement of multiconformer ensemble models from multi-temperature X-ray diffraction data.Methods in enzymology · 2023Article
- Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals.Acta crystallographica. Section D, Structural biology · 2022Article
- Determination of the through-plane profile of vanadium species in hydrated Nafion studied with micro X-ray absorption near-edge structure spectroscopy - proof of concept.Journal of synchrotron radiation · 2021Article
- Analysis of complex, beam-sensitive materials by transmission electron microscopy and associated techniques.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020Article
- Instrumentation and experimental procedures for robust collection of X-ray diffraction data from protein crystals across physiological temperatures.Journal of applied crystallography · 2020Article
- Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Solvent flows, conformation changes and lattice reordering in a cold protein crystal.Acta crystallographica. Section D, Structural biology · 2019Article
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- Sample manipulation and data assembly for robust microcrystal synchrotron crystallography.IUCrJ · 2018Article
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- Conformational variation of proteins at room temperature is not dominated by radiation damage.Journal of synchrotron radiation · 2017Article
- Temperature-dependent radiation sensitivity and order of 70S ribosome crystals.Acta crystallographica. Section D, Biological crystallography · 2014Article
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2 authors at 1 institution in 1 country.
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Abstract
The temperature-dependence of radiation damage to thaumatin crystals between T = 300 and 100 K is reported. The amount of damage for a given dose decreases sharply as the temperature decreases from 300 to 220 K and then decreases more gradually on further cooling below the protein-solvent glass transition. Two regimes of temperature-activated behavior were observed. At temperatures above ∼200 K the activation energy of 18.0 kJ mol(-1) indicates that radiation damage is dominated by diffusive motions in the protein and solvent. At temperatures below ∼200 K the activation energy is only 1.00 kJ mol(-1), which is of the order of the thermal energy. Similar activation energies describe the temperature-dependence of radiation damage to a variety of solvent-free small-molecule organic crystals over the temperature range T = 300-80 K. It is suggested that radiation damage in this regime is vibrationally assisted and that the freezing-out of amino-acid scale vibrations contributes to the very weak temperature-dependence of radiation damage below ∼80 K. Analysis using the radiation-damage model of Blake and Phillips [Blake & Phillips (1962), Biological Effects of Ionizing Radiation at the Molecular Level, pp. 183-191] indicates that large-scale conformational and molecular motions are frozen out below T = 200 K but become increasingly prevalent and make an increasing contribution to damage at higher temperatures. Possible alternative mechanisms for radiation damage involving the formation of hydrogen-gas bubbles are discussed and discounted. These results have implications for mechanistic studies of proteins and for studies of the protein glass transition. They also suggest that data collection at T ≃ 220 K may provide a viable alternative for structure determination when cooling-induced disorder at T = 100 is excessive.
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