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When FT-IR spectroscopy meets X-ray crystallography

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The first time-resolved FT-IR spectroscopic study of the photoactive yellow protein addresses the conflict between the X-ray structures of two early photocycle intermediates.

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Figure 1: Overall structure of the photoactive yellow protein.
Figure 2: Photocycle of the photoactive yellow protein.
Figure 3: The carbonyl stretching vibration of carboxylic amino acid side chains.
Figure 4: Sequence of structural changes in the active site of PYP (CPK color coding).

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Acknowledgements

We thank G. Büldt and J. Labahn for helpful discussions on the interpretation of X-ray diffraction data.

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Author notes

  1. Joachim Heberle and Thomas Gensch: J.H. is in Structural Biology and T.G. is in Cellular Signal Processing.

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  1. the Forschungszentrum Jülich, Jülich, 52425, Germany

    Joachim Heberle & Thomas Gensch

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  1. Joachim Heberle
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Correspondence to Joachim Heberle.

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Heberle, J., Gensch, T. When FT-IR spectroscopy meets X-ray crystallography. Nat Struct Mol Biol 8, 195–197 (2001). https://doi.org/10.1038/84909

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