A method has been devised that extends the resolution of X-ray crystal structures beyond the diffraction limit. This might help to improve the visualization of structures of proteins that form 'poorly diffracting' crystals. See Letter p.202
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References
Bragg, W. L. Proc. Cambr. Phil. Soc. 17, 43–57 (1913).
Ayyer, K. et al. Nature 530, 202–206 (2016).
Pérez, J., Faure, P. & Benoit, J.-P. Acta Crystallogr. D 52, 722–729 (1996).
Welberry, T. R., Heerdegen, A. P., Goldstone, D. C. & Taylor, I. A. Acta Crystallogr. B 67, 516–524 (2011).
Miao, J., Ishikawa, T., Robinson, I. K. & Murnane, M. M. Science 348, 530–535 (2015).
Elser, V. J. Opt. Soc. Am. A 20, 40–55 (2003).
Elser, V. & Millane, R. P. Acta Crystallogr. A 64, 273–279 (2008).
Fischer, N. et al. Nature 520, 567–570 (2015).
Umena, Y., Kawakami, K., Shen, J.-R., & Kamiya, N. Nature 473, 55–60 (2011).
Suga, M. et al. Nature 517, 99–103 (2015).
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Shen, JR. Resolution beyond the diffraction limit. Nature 530, 168–169 (2016). https://doi.org/10.1038/530168a
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DOI: https://doi.org/10.1038/530168a
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