High-resolution structure determination by continuous-rotation data collection in MicroED

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroED in structural biology.

Original languageEnglish (US)
Pages (from-to)927-930
Number of pages4
JournalNature Methods
Volume11
Issue number9
DOIs
StatePublished - Sep 1 2014
Externally publishedYes

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Microcrystals
Muramidase
Electron diffraction
Proteins
Software
Electrons
Network protocols
Crystals

ASJC Scopus subject areas

  • Medicine(all)

Cite this

High-resolution structure determination by continuous-rotation data collection in MicroED. / Nannenga, Brent.

In: Nature Methods, Vol. 11, No. 9, 01.09.2014, p. 927-930.

Research output: Contribution to journalArticle

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