High resolution structure of deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution*

HIGHLIGHTS

• who: Jeremiah R. Wagner from the EXPERIMENTAL PROCEDURES Protein Production and Crystallization-DrCBD encompassing the first , amino acids of DrBphP and containing an, terminal , tag and a, terminal His, tag was as described (9)DrCBD-Y S was generated by correcting the inadvertent point mutation that substituted Pro, for a Thr and converting the Tyr, codon to that for a serine with the QuikChange method (Stratagene, La Jolla, CA). The DrCBD-Y S apoprotein was expressed in Escherichia coli strain Rosetta (DE3) (Novagen, San Diego, CA) with or without simultaneous expression of the heme oxygenase from Synechocystis . . .
  

   

  

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