ArticleActa crystallographica. Section D, Biological crystallography2015
Radiation decay of thaumatin crystals at three X-ray energies.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Separating the effects of temperature and absorbed X-ray dose on unit-cell volume.Acta crystallographica. Section D, Structural biology · 2026Article
- Damage-limited resolution for X-ray and electron microscopy of organic specimens.Acta crystallographica. Section D, Structural biology · 2026Article
- Limiting the effects of radiation damage in MicroED through dose selection during data processing.Acta crystallographica. Section D, Structural biology · 2025Article
- Variability in X-ray induced effects in [Rh(COD)Cl]Physical chemistry chemical physics : PCCP · 2022Article
- Cryo-electron tomography related radiation-damage parameters for individual-molecule 3D structure determination.Frontiers in chemistry · 2022Review
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- Low-dose X-ray structure analysis of cytochrome c oxidase utilizing high-energy X-rays.Journal of synchrotron radiation · 2019Article
- Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics.International journal of molecular sciences · 2018Review
- X-ray-induced sample damage at the Mn L-edge: a case study for soft X-ray spectroscopy of transition metal complexes in solution.Physical chemistry chemical physics : PCCP · 2018Article
- Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.Structure (London, England : 1993) · 2018Article
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- The hidden treasure in your data: phasing with unexpected weak anomalous scatterers from routine data sets.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Development of a dose-limiting data collection strategy for serial synchrotron rotation crystallography.Journal of synchrotron radiation · 2017Article
- RNA protects a nucleoprotein complex against radiation damage.Acta crystallographica. Section D, Structural biology · 2016Article
- Objective evaluation of radiation damage in a nucleoprotein complex.Acta crystallographica. Section D, Structural biology · 2016Article
- In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures.Acta crystallographica. Section D, Structural biology · 2016Article
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Abstract
Radiation damage is an unavoidable obstacle in X-ray crystallographic data collection for macromolecular structure determination, so it is important to know how much radiation a sample can endure before being degraded beyond an acceptable limit. In the literature, the threshold at which the average intensity of all recorded reflections decreases to a certain fraction of the initial value is called the `dose limit'. The first estimated D50 dose-limit value, at which the average diffracted intensity was reduced to 50%, was 20 MGy and was derived from observing sample decay in electron-diffraction experiments. A later X-ray study carried out at 100 K on ferritin protein crystals arrived at a D50 of 43 MGy, and recommended an intensity reduction of protein reflections to 70%, D70, corresponding to an absorbed dose of 30 MGy, as a more appropriate limit for macromolecular crystallography. In the macromolecular crystallography community, the rate of intensity decay with dose was then assumed to be similar for all protein crystals. A series of diffraction images of cryocooled (100 K) thaumatin crystals at identical small, 2° rotation intervals were recorded at X-ray energies of 6.33 , 12.66 and 19.00 keV. Five crystals were used for each wavelength. The decay in the average diffraction intensity to 70% of the initial value, for data extending to 2.45 Å resolution, was determined to be about 7.5 MGy at 6.33 keV and about 11 MGy at the two higher energies.
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