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Related Experiment Videos

His-tag impact on structure.

Mike Carson1, David H Johnson, Heather McDonald

  • 1Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, 251 CBSE, 1025 18th Street South, Birmingham, AL 35294-4400, USA. carson@uab.edu

Acta Crystallographica. Section D, Biological Crystallography
|March 1, 2007
PubMed
Summary
This summary is machine-generated.

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His tags generally do not affect protein structure, though higher resolution is seen when tags are resolved in crystal structures. Further PDB annotation is recommended.

Area of Science:

  • Structural biology
  • Biochemistry
  • Protein crystallography

Background:

  • Protein constructs often include His tags for purification.
  • The impact of His tags on native protein structure is often assumed to be negligible.

Purpose of the Study:

  • To survey and compare crystal structures with and without His tags.
  • To assess the effect of His tags on protein structure and crystallographic data.

Main Methods:

  • Comparative analysis of PDB crystal structures.
  • Examination of refined tag residues within electron density.
  • Assessment of resolution, R factors, and B factors.

Main Results:

  • His tag residues are refined into density in less than 10% of tagged structures.

Related Experiment Videos

  • Higher resolution crystals are observed when His tags are resolved.
  • No significant effect on native protein structure, resolution, or R factors.
  • Slightly higher overall B factors observed in tagged structures.
  • Conclusions:

    • His tags generally do not significantly alter the native protein structure.
    • The presence of resolved His tags correlates with improved crystal resolution.
    • Explicit annotation of His tags in PDB format is recommended for clarity.