uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Serial Femtosecond Crystallography of G Protein-Coupled Receptors
Show others and affiliations
2013 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 342, no 6165, 1521-1524 p.Article in journal (Refereed) Published
Abstract [en]

X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.

Place, publisher, year, edition, pages
2013. Vol. 342, no 6165, 1521-1524 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-217630DOI: 10.1126/science.1244142ISI: 000328644300062OAI: oai:DiVA.org:uu-217630DiVA: diva2:694294
Available from: 2014-02-06 Created: 2014-02-04 Last updated: 2014-10-01Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Seibert, M. Marvin
By organisation
Molecular biophysics
In the same journal
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 180 hits
ReferencesLink to record
Permanent link

Direct link