Journal Article/Journal Article PHPPUBDB-22476

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High-resolution protein structure determination by serial femtosecond crystallography

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2012

Science 337, 362-364 () [10.1126/science.1217737]
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Abstract: Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

Keyword(s): Animals (MeSH) ; Crystallography, X-Ray: methods (MeSH) ; Lasers (MeSH) ; Muramidase: chemistry (MeSH) ; Muramidase: radiation effects (MeSH) ; Protein Conformation (MeSH) ; hen egg lysozyme ; Muramidase


Contributing Institute(s):
  1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
  2. Forschungsgruppe für strukturelle Dynamik (MPSD)
Research Program(s):
  1. Experiments at CFEL (POF2-544) (POF2-544)
Experiment(s):
  1. Experiments at CFEL

Appears in the scientific report 2012
Notes: First published online in Science Express on 31. May 2012. Final "paper" version published in "main" Science on 20. July 2012.
Database coverage:
Medline ; OpenAccess ; BIOSIS Previews ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; JCR ; NCBI Molecular Biology Database ; No Author Disambiguation ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record
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Private Collections > >DESY > >FS > FS-CFEL-1
Document types > Articles > Journal Article
Private Collections > >MPG > MPSD
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 Record created 2013-01-18, last modified 2025-07-18


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