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A generic cross-seeding approach to protein crystallization.

Ido Caspy1, Shan Tang2, Dom Bellini1

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, CambridgeCB2 0QH, United Kingdom.

Journal of Applied Crystallography
|April 2, 2025
PubMed
Summary

This study introduces a novel cross-seeding method using generic protein crystal fragments to overcome crystallization challenges in X-ray crystallography. This approach successfully yielded diffraction-quality crystals for retinoblastoma binding protein 9, advancing structural biology.

Keywords:
X-ray crystallographycross-seedingmacromolecular crystallizationnucleationprotein crystals

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Crystallization is a bottleneck in determining biological macromolecule structures via X-ray crystallography.
  • Generic seeding strategies are needed to improve crystallization success rates.

Purpose of the Study:

  • To investigate a cross-seeding approach using a heterogeneous mixture of protein crystal fragments as generic seeds.
  • To obtain diffraction-quality crystals of human serine hydrolase retinoblastoma binding protein 9 (RBBP9) for structure determination.

Main Methods:

  • Development and application of a novel cross-seeding mixture containing nanometre-sized protein crystal fragments.
  • Standard crystallization assays were performed with the protein sample and the seeding mixture.
  • X-ray crystallography was used to solve the structure of RBBP9 at 1.4 Å resolution.

Main Results:

  • An atypical crystal form of RBBP9 was successfully obtained using the cross-seeding mixture.
  • The crystal structure of RBBP9 was determined at high resolution (1.4 Å).
  • Follow-up experiments identified α-amylase crystal fragments as critical for this specific crystallization success.

Conclusions:

  • The developed cross-seeding method offers a promising strategy to overcome crystallization challenges in structural biology.
  • This technique can facilitate structure determination of challenging protein targets.
  • Further research is needed to explore the limitations and broader applications of this generic seeding approach.