ArticleProtein science : a publication of the Protein Society2016
Oxygen additions in serial femtosecond crystallographic protein structures.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 14 citations in OpenAlex.
- An analysis of the structural changes of the oxygen evolving complex of Photosystem II in the SBiochimica et biophysica acta. Bioenergetics · 2025Review
- All polymer microfluidic chips-A fixed target sample delivery workhorse for serial crystallography.Biomicrofluidics · 2023Article
- How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM.Journal of structural biology · 2022Article
- Crystal structure of the C-terminal domain of DENR.Computational and structural biotechnology journal · 2020Article
- Crystallographic identification of spontaneous oxidation intermediates and products of protein sulfhydryl groups.Protein science : a publication of the Protein Society · 2019Article
- On the damage done to the structure of the Thermoplasma acidophilum proteasome by electron radiation.Protein science : a publication of the Protein Society · 2018Article
- Atomic resolution structure of serine protease proteinase K at ambient temperature.Scientific reports · 2017Article
- Insights into Photosystem II from Isomorphous Difference Fourier Maps of Femtosecond X-ray Diffraction Data and Quantum Mechanics/Molecular Mechanics Structural Models.ACS energy letters · 2017Review
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Abstract
In principle, serial femtosecond crystallography (SFX) could yield data sets that are completely free of the effects caused by slow, radiation-induced chemical reactions, for example, oxygen additions, responsible for radiation damage. However, experimental evidence is presented here that SFX data sets obtained by techniques that expose different parts of the same specimen to single pulses of radiation do not have this property, even if the specimen in question is frozen. The diffraction image of each such crystal obtained with the first pulse of radiation is certain to represent the structure of a protein that has not been modified chemically, but all of the images obtained subsequently from the same crystal will represent structures that have been modified to a lesser or greater extent by oxygen additions because of the rapid diffusion of oxygenic free radicals through the specimen. The higher the level of oxygen additions a crystal suffers during data collection, the poorer the statistical quality of data set obtained from it will, and the higher the free R-factors of the resulting structural model.
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