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The MORPHEUS II protein crystallization screen.

Fabrice Gorrec1

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, England.

Acta Crystallographica. Section F, Structural Biology Communications
|July 7, 2015
PubMed
Summary
This summary is machine-generated.

A new crystallization screen, MORPHEUS II, enhances protein structure determination by improving crystal yield. This novel formulation aids in obtaining diffraction-quality crystals, even for challenging protein samples.

Keywords:
MORPHEUS IIcrystallization additivescrystallization screeningheavy-atom derivatizationmacromolecular crystallographyprotein crystallization

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Area of Science:

  • Structural biology
  • Biochemistry
  • Crystallography

Background:

  • High-quality crystals are essential for X-ray diffraction-based protein structure determination.
  • Traditional crystallization screens often yield low success rates for obtaining diffraction-quality crystals.
  • Innovative screening formulations are needed to improve crystal formation efficiency.

Purpose of the Study:

  • To introduce MORPHEUS II, an advanced crystallization screen designed to overcome limitations of traditional methods.
  • To develop novel crystallization conditions that increase the yield of diffraction-quality crystals.
  • To incorporate reagents for experimental phasing and cryoprotection within the screen.

Main Methods:

  • Development of MORPHEUS II, a 96-condition screen building upon the original MORPHEUS formulation.
  • Selection of reagents including additives from the Protein Data Bank, cryoprotectants, and buffer systems.
  • Inclusion of heavy atoms for experimental phasing and small polyols for cryoprotection.

Main Results:

  • MORPHEUS II demonstrated suitability for crystallizing a diverse range of protein samples.
  • The novel conditions within MORPHEUS II were effective in cases where traditional screens failed.
  • The efficiency of MORPHEUS II was evaluated and compared against commercially available crystallization screens.

Conclusions:

  • MORPHEUS II represents a significant advancement in crystallization screening for protein structure determination.
  • The screen's design facilitates the acquisition of diffraction-quality crystals, particularly for recalcitrant proteins.
  • MORPHEUS II offers a valuable tool for structural biologists seeking to improve crystallization outcomes.