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Related Experiment Videos

MAD phasing with krypton.

A Cohen1, P Ellis, N Kresge

  • 1The Stanford Synchrotron Research Laboratory, SLAC, PO Box 4349, Bin 99, Stanford University, CA 94309, USA.

Acta Crystallographica. Section D, Biological Crystallography
|February 15, 2001
PubMed
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Krypton (Kr) K-edge multi-wavelength anomalous diffraction (MAD) is a feasible method for routine protein structure determination. This technique allows for single-crystal phasing, offering an accessible alternative to xenon (Xe) for derivatization and structural analysis.

Area of Science:

  • Structural biology
  • X-ray crystallography
  • Biophysics

Background:

  • Multi-wavelength anomalous diffraction (MAD) is crucial for protein structure determination.
  • Xenon (Xe) derivatization is useful but its edges are not ideal for MAD.
  • Krypton (Kr) offers an accessible K edge (14.3 keV) for MAD experiments.

Purpose of the Study:

  • To demonstrate the feasibility of Kr K-edge MAD as a routine method for protein structure determination.
  • To present Kr derivatization as a viable alternative to Xe for MAD phasing.
  • To showcase single-crystal phasing using Kr MAD.

Main Methods:

  • Protein crystals were derivatized by pressurization with Kr gas.
  • Three-wavelength data were collected at SSRL beamline 9-2.

Related Experiment Videos

  • MAD phases were calculated using SHARP and refined with wARP.

    • Main Results:

    • Successful phasing of two proteins, myoglobin (Mb) and SP18, using Kr MAD.
    • Kr derivatization was achieved in approximately 50% of protein crystals tested.
    • Excellent quality electron density maps were obtained for both Mb and SP18.

    Conclusions:

    • Kr K-edge MAD is a practical and effective method for routine protein structure determination.
    • Kr derivatization provides a single-crystal phasing solution accessible on most MAD beamlines.
    • This method enhances structural biology capabilities by offering an alternative to existing techniques.