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- W2588893844 abstract "Significance The room temperature structure of natively formed protein nanocrystals consisting of 9,000 unit cells has been solved to 2 Å resolution using an unattenuated X-ray free-electron laser (XFEL) beam, representing, by far, the smallest protein crystals used for protein structure determination by X-ray crystallography to date. Radiation damage limits structure determination from protein crystals using synchrotron techniques, whereas femtosecond X-ray pulses from free-electron lasers enable much higher tolerable doses, extracting more signal per molecule, allowing the study of submicrometer crystals. Radiation-sensitive features, such as disulfide bonds, are well resolved in the XFEL structure despite the extremely high dose (1.3 GGy) used. Analysis of signal levels obtained in this experiment indicates that structure determination from even smaller protein crystals could be possible." @default.
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- W2588893844 date "2017-02-15" @default.
- W2588893844 modified "2023-10-12" @default.
- W2588893844 title "Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser" @default.
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- W2588893844 doi "https://doi.org/10.1073/pnas.1609243114" @default.
- W2588893844 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5338516" @default.
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- W2588893844 hasPublicationYear "2017" @default.
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