On the state of crystallography at the dawn of the electron microscopy revolution

Matthew K. Higgins, Susan M. Lea

Research output: Contribution to journalArticleOtherpeer-review

6 Citations (Scopus)


While protein crystallography has, for many years, been the most used method for structural analysis of macromolecular complexes, remarkable recent advances in high-resolution electron cryo-microscopy led to suggestions that ‘the revolution will not be crystallised’. Here we highlight the current success rate, speed and ease of modern crystallographic structure determination and some recent triumphs of both ‘classical’ crystallography and the use of X-ray free electron lasers. We also outline fundamental differences between structure determination using X-ray crystallography and electron microscopy. We suggest that crystallography will continue to co-exist with electron microscopy as part of an integrated array of methods, allowing structural biologists to focus on fundamental biological questions rather than being constrained by the methods available.

Original languageEnglish
Pages (from-to)95-101
Number of pages7
JournalCurrent Opinion in Structural Biology
Publication statusPublished - Oct 2017
Externally publishedYes

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