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Related Experiment Videos

Protein crystallization by design: chymotrypsinogen without precipitants.

P E Pjura1, A M Lenhoff, S A Leonard

  • 1Center for Molecular and Engineering Thermodynamics, Department of Chemical Engineering, University of Delaware, Newark, DE 19716, USA.

Journal of Molecular Biology
|June 30, 2000
PubMed
Summary

Researchers developed a systematic method for protein crystallization, yielding high-quality crystals of bovine chymotrypsinogen A. This predictive approach avoids empirical screening and expands crystallization possibilities.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Protein crystallization typically relies on empirical screening.
  • Existing bovine chymotrypsinogen A structures were determined using ethanol-containing solutions.

Purpose of the Study:

  • To develop and apply a systematic predictive procedure for protein crystallization.
  • To obtain high-resolution X-ray structure of bovine chymotrypsinogen A using novel conditions.

Main Methods:

  • Measurements of osmotic second virial coefficient to determine suitable solvent conditions.
  • Ultracentrifugal crystallization for approximately 30 hours without precipitants.
  • X-ray structure determination to 3 Å resolution.

Main Results:

Related Experiment Videos

  • Data-quality crystals of bovine chymotrypsinogen A were produced using buffered NaCl solutions.
  • A refined X-ray structure was obtained with high map quality, defining most protein atoms.
  • Crystallization occurred in the tetragonal space group P4(1)2(1)2.

Conclusions:

  • A systematic, predictive approach to protein crystallization is feasible.
  • This method expands the range of successful crystallization conditions and can yield new crystal forms.
  • Observed minor structural differences suggest potential effects of prior crystallization conditions.