Sep 21, 2012

The structures of T6, T3R3 and R6 bovine insulin: combining X-ray diffraction and absorption spectroscopy

Acta Crystallographica. Section D, Biological Crystallography
Christian Grundahl FrankærPernille Harris

Abstract

The crystal structures of three conformations, T(6), T(3)R(3) and R(6), of bovine insulin were solved at 1.40, 1.30 and 1.80 Å resolution, respectively. All conformations crystallized in space group R3. In contrast to the T(6) and T(3)R(3) structures, different conformations of the N-terminal B-chain residue PheB1 were observed in the R(6) insulin structure, resulting in an eightfold doubling of the unit-cell volume upon cooling. The zinc coordination in each conformation was studied by X-ray absorption spectroscopy (XAS), including both EXAFS and XANES. Zinc adopts a tetrahedral coordination in all R(3) sites and an octahedral coordination in T(3) sites. The coordination distances were refined from XAS with a standard deviation of <0.01 Å. In contrast to the distances determined from the medium-resolution crystal structures, the XAS results were in good agreement with similar coordination geometries found in small molecules, as well as in other high-resolution insulin structures. As the radiation dose for XRD experiments is two orders of magnitude higher compared with that of XAS experiments, the single crystals were exposed to a higher degree of radiation damage that affected the zinc coordination in the T(3) sites in particu...Continue Reading

  • References31
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References

  • References31
  • Citations4

Citations

Mentioned in this Paper

Crystal - Body Material
Insulin, Beef
Crystallography, X-Ray
X-Ray Diffraction
Protein Multimerization
Protein Conformation
Novolin
Crystal Structure
Near Edge X-Ray Absorption Fine Structure Spectroscopy
Spectrum Analysis

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