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Femtosecond X-ray diffraction from two-dimensional protein crystals
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2014 (English)In: IUCrJ, ISSN 2052-2525, Vol. 1, no 2, 95-100 p.Article in journal (Refereed) Published
Abstract [en]

X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.

Place, publisher, year, edition, pages
2014. Vol. 1, no 2, 95-100 p.
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Structural Biology
URN: urn:nbn:se:uu:diva-232832DOI: 10.1107/S2052252514001444PubMedID: 25075325OAI: oai:DiVA.org:uu-232832DiVA: diva2:749968
Available from: 2014-09-25 Created: 2014-09-25 Last updated: 2014-10-01Bibliographically approved

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Seibert, M Marvin
Structural Biology

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