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Protein structure determination by electron diffraction using a single three-dimensional nanocrystal
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för material- och miljökemi (MMK).
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Rekke forfattare: 6
2017 (engelsk)Inngår i: Acta Crystallographica Section D Structural Biology, ISSN 2059-7983, Vol. 73, 738-748 s.Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Three-dimensional nanometre-sized crystals of macromolecules currently resist structure elucidation by single-crystal X-ray crystallography. Here, a single nanocrystal with a diffracting volume of only 0.14 mu m(3), i.e. no more than 6 x 10(5) unit cells, provided sufficient information to determine the structure of a rare dimeric polymorph of hen egg-white lysozyme by electron crystallography. This is at least an order of magnitude smaller than was previously possible. The molecular-replacement solution, based on a monomeric polyalanine model, provided sufficient phasing power to show side-chain density, and automated model building was used to reconstruct the side chains. Diffraction data were acquired using the rotation method with parallel beam diffraction on a Titan Krios transmission electron microscope equipped with a novel in-house-designed 1024 x 1024 pixel Timepix hybrid pixel detector for low-dose diffraction data collection. Favourable detector characteristics include the ability to accurately discriminate single high-energy electrons from X-rays and count them, fast readout to finely sample reciprocal space and a high dynamic range. This work, together with other recent milestones, suggests that electron crystallography can provide an attractive alternative in determining biological structures.

sted, utgiver, år, opplag, sider
2017. Vol. 73, 738-748 s.
Emneord [en]
electron crystallography, protein nanocrystals, hybrid pixel detector
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-146975DOI: 10.1107/S2059798317010348ISI: 000409298200003OAI: oai:DiVA.org:su-146975DiVA: diva2:1142077
Tilgjengelig fra: 2017-09-18 Laget: 2017-09-18 Sist oppdatert: 2017-09-18bibliografisk kontrollert

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