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Comparing serial X-ray crystallography and microcrystal electron diffraction (MicroED) as methods for routine structure determination from small macromolecular crystals

By Alexander M. Wolff, Iris Diane Young1, Raymond G. Sierra, Aaron S. Brewster, Michael W. Martynowycz, Eriko Nango, Michihiro Sugahara, Takanori Nakane, Kazutaka Ito, Andrew Aquila, Asmit Bhowmick, Justin T. Biel, Sergio Carbajo, Aina E. Cohen, Saul Cortez, Ana Gonzalez, Tomoya Hino, Dohyun Im, Jake D. Koralek, Minoru Kubo, Tomas Lazarou2, Takashi Nomura, Shigeki Owada, Avi J. Samelson, Tomoyuki Tanaka, Rie Tanaka, Erin M. Thompson, Henry Van Den Bedem, Rahel Woldeyes1, Fumiaki Yumoto, Wei Zhao, Kensuke Tono, Sebastien Boutet, So Iwata, Tamir Gonen, Nicholas K. Sauter, James Fraser3, Michael Thompson1

1. University of California - San Francisco 2. McMaster University 3. University of California-San Francisco

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

Alexander M. Wolff and Iris D. Young and Raymond G. Sierra and Aaron S. Brewster and Michael W. Martynowycz and Eriko Nango and Michihiro Sugahara and Takanori Nakane and Kazutaka Ito and Andrew Aquila and Asmit Bhowmick and Justin T. Biel and Sergio Carbajo and Aina E. Cohen and Saul Cortez and Ana Gonzalez and Tomoya Hino and Dohyun Im and Jake D. Koralek and Minoru Kubo and Tomas S. Lazarou and Takashi Nomura and Shigeki Owada and Avi J. Samelson and Tomoyuki Tanaka and Rie Tanaka and Erin M. Thompson and Henry van den Bedem and Rahel A. Woldeyes and Fumiaki Yumoto and Wei Zhao and Kensuke Tono and Sebastien Boutet and So Iwata and Tamir Gonen and Nicholas K. Sauter and James S. Fraser and Michael C. Thompson

Citation

Wolff, A.M. et al., 2020. Comparing serial X-ray crystallography and microcrystal electron diffraction (MicroED) as methods for routine structure determination from small macromolecular crystals. IUCrJ, 7(2), pp.306–323. Available at: http://dx.doi.org/10.1107/s205225252000072x.

Abstract

Innovative new crystallographic methods are facilitating structural studies from ever smaller crystals of biological macromolecules. In particular, serial X-ray crystallography and microcrystal electron diffraction (MicroED) have emerged as useful methods for obtaining structural information from crystals on the nanometre to micrometre scale. Despite the utility of these methods, their implementation can often be difficult, as they present many challenges that are not encountered in traditional macromolecular crystallography experiments. Here, XFEL serial crystallography experiments and MicroED experiments using batch-grown microcrystals of the enzyme cyclophilin A are described. The results provide a roadmap for researchers hoping to design macromolecular microcrystallography experiments, and they highlight the strengths and weaknesses of the two methods. Specifically, we focus on how the different physical conditions imposed by the sample-preparation and delivery methods required for each type of experiment affect the crystal structure of the enzyme.

DOI

http://dx.doi.org/10.1107/s205225252000072x

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)