Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

S Botha1,2,3, D Baitan1,2,4, K E J Jungnickel1

  • 1Institute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.

Iucrj
|September 19, 2018
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors.

Nature communications·2020
Same author

Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate.

Acta crystallographica. Section F, Structural biology communications·2018
Same author

Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse.

Structural dynamics (Melville, N.Y.)·2016
Same author

Real-time investigation of dynamic protein crystallization in living cells.

Structural dynamics (Melville, N.Y.)·2016
Same author

Crystallographic portrayal of different conformational states of a Lys49 phospholipase A₂ homologue: insights into structural determinants for myotoxicity and dimeric configuration.

International journal of biological macromolecules·2012
Same author

Structural insights into selectivity and cofactor binding in snake venom L-amino acid oxidases.

Biochemical and biophysical research communications·2012
Same journal

Towards light-coupled sample preparation for time-resolved cryoEM studies.

IUCrJ·2026
Same journal

Cryo-EM analysis of cooperative conformational changes in the SARS-CoV-2 spike protein trimer.

IUCrJ·2026
Same journal

Towards time-resolved MicroED grid preparation using mix-and-inject gas dynamic virtual nozzles.

IUCrJ·2026
Same journal

How cryoEM has advanced our understanding of bacteriophages and bacteriocins targeting Clostridioides difficile.

IUCrJ·2026
Same journal

CryoEM structures reveal allosteric regulation of the catalytic activity of the multi-protein human MAT enzyme complexes.

IUCrJ·2026
Same journal

Cryo-EM-guided subtractive optimization of a novel VCP/p97 inhibitor.

IUCrJ·2026
See all related articles
This summary is machine-generated.

Researchers developed a gentle method using lipidic cubic phase (LCP) for heavy atom incorporation in serial crystallography. This technique enables efficient experimental phasing and accurate protein structure determination, even with limited diffraction data.

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Serial crystallography has advanced significantly, with data collection established at synchrotron and XFEL sources.
  • Experimental phasing for serial crystallography remains challenging due to data inaccuracies.

Purpose of the Study:

  • To develop a gentle and efficient method for incorporating heavy atoms into microcrystals for serial crystallography.
  • To improve experimental phasing capabilities for serial crystallography data.

Main Methods:

  • Utilized lipidic cubic phase (LCP) as a carrier medium for heavy atom incorporation into micrometre-sized crystals.
  • Employed synchrotron radiation and mercury's anomalous scattering for single isomorphous replacement with anomalous scattering (SIRAS) phasing.
  • Applied automatic model-building tools for structural analysis.
Keywords:
SIRAS phasingde novo protein structure determinationheavy-atom soakinglipidic cubic phaseserial crystallography

Related Experiment Videos

Main Results:

  • Demonstrated a gentle and efficient approach for preparing heavy-atom-derivative crystals prior to data collection.
  • Achieved effective phasing using a low number of diffraction patterns.
  • Generated high-quality electron-density maps sufficient for complete model building.
  • Determined the structure of proteinase K at 1.9 Å resolution.

Conclusions:

  • The LCP-based heavy atom soaking method is a viable strategy for serial crystallography.
  • This approach facilitates experimental phasing and accurate structure determination.
  • Enables high-resolution structural analysis of proteins using serial crystallography.