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Updated structure of Drosophila cryptochrome

Author

Listed:
  • Colin Levy

    (*Manchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK)

  • Brian D. Zoltowski

    (Cornell University)

  • Alex R. Jones

    (*Manchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK)

  • Anand T. Vaidya

    (Cornell University)

  • Deniz Top

    (Laboratory of Genetics, The Rockefeller University)

  • Joanne Widom

    (Cornell University)

  • Michael W. Young

    (Laboratory of Genetics, The Rockefeller University)

  • Nigel S. Scrutton

    (*Manchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK)

  • Brian R. Crane

    (Cornell University)

  • David Leys

    (*Manchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK)

Abstract

Arising from B. D. Zoltowski et al. Nature 480, 396–399 (2011)10.1038/nature10618 Recently, we determined the X-ray crystal structure of full-length cryptochrome from Drosophila1. Here we report an improved model of the Drosophila cryptochrome (dCRY) structure that corrects errors in the original coordinates (Protein Data Bank (PDB) accession 3TVS). Further refinement of the structure, with automated rebuilding algorithms in Phenix2 followed by manual building, indicated that a model of dCRY could be produced with excellent refinement statistics without taking into account the non-merohedral twinning originally reported (Table 1). Table 1 Data collection and phasing statistics Native Data collection 0.97918 Space group P21 Cell dimensions a, b, c (Å) 72.8, 112.3, 75.0 α, β, γ 90.0, 114.9, 90.0 Resolution (Å) 30–2.30 (2.38–2.30)* R sym 0.126 (0.354) I/σ (I) 11.9 (1.8) Completeness (%) 90.1 (57.3) Redundancy 3.9 Refinement 3TVS (detwinned/native) Rebuilt (detwinned/native) Resolution (Å) 30–2.3 (2.30–2.38)* 30–2.3 Å (2.30–2.38)* Number of reflections 47,507 47,507 Rwork (%) 25.3 (30.0)/34.2 (43.9) 22.2 (24.4)/18.4 (24.2) Rfree (%) 29.8 (35.8)/40.5 (49.3) 26.0 (34.2)/24.7 (32.1) Protein 8,668 8,653 Solvent 301 321 Ligand (FAD/Mg) 106/2 106/2 B-factors (Å2) Protein 38.1 32.2 Ligand (FAD/Mg) 10.0 18.1 Water 28.6 30.7 r.m.s.d. Bond lengths (Å) 0.01 0.008 Bond angles (°) 1.8 1.1 Revised data collection and Phenix refinement statistics (corrected Supplementary Table 2 from ref. 1). *Highest resolution bin for compiling statistics.

Suggested Citation

  • Colin Levy & Brian D. Zoltowski & Alex R. Jones & Anand T. Vaidya & Deniz Top & Joanne Widom & Michael W. Young & Nigel S. Scrutton & Brian R. Crane & David Leys, 2013. "Updated structure of Drosophila cryptochrome," Nature, Nature, vol. 495(7441), pages 3-4, March.
    • Handle: RePEc:nat:nature:v:495:y:2013:i:7441:d:10.1038_nature11995
    DOI: 10.1038/nature11995
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    Cited by:

    1. Sahar Foroutannejad & Lydia L. Good & Changfan Lin & Zachariah I. Carter & Mahlet G. Tadesse & Aaron L. Lucius & Brian R. Crane & Rodrigo A. Maillard, 2023. "The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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