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

Alexander M WolffIris D YoungRaymond G SierraAaron S BrewsterMichael W MartynowyczEriko NangoMichihiro SugaharaTakanori NakaneKazutaka ItoAndrew AquilaAsmit BhowmickJustin T BielSergio CarbajoAina E CohenSaul CortezAna GonzalezTomoya HinoDohyun ImJake D KoralekMinoru KuboTomas S LazarouTakashi NomuraShigeki OwadaAvi J SamelsonTomoyuki TanakaRie TanakaErin M ThompsonHenry van den BedemRahel A WoldeyesFumiaki YumotoWei ZhaoKensure TonoSébastien BoutetSo IwataTamir GonenNicholas K SauterBrian K ShoichetMichael C Thompson
Published in: IUCrJ (2020)
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.
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