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

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Femtosecond X-ray protein nanocrystallography
Show others and affiliations
2011 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 470, no 7332, 73-77 p.Article in journal (Refereed) Published
Abstract [en]

X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded(1-3). It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction 'snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source(4). We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes(5). More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (similar to 200 nm to 2 mm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes(6). This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage.

Place, publisher, year, edition, pages
2011. Vol. 470, no 7332, 73-77 p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-146068DOI: 10.1038/nature09750ISI: 000286886400036PubMedID: 21293373OAI: oai:DiVA.org:uu-146068DiVA: diva2:397618
Available from: 2011-02-15 Created: 2011-02-15 Last updated: 2017-12-11

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

Maia, Filipe R. N. C.Caleman, CarlHajdu, JanosTimneanu, NicusorSeibert, M. MarvinAndreasson, JakobJönsson, OlofSvenda, MartinAndersson, Inger

Search in DiVA

By author/editor
Maia, Filipe R. N. C.Caleman, CarlHajdu, JanosTimneanu, NicusorSeibert, M. MarvinAndreasson, JakobJönsson, OlofSvenda, MartinAndersson, Inger
By organisation
Molecular biophysics
In the same journal
Nature
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 516 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf