Plant Photomorphogenesis: A green light for cryptochrome research

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Plant Photomorphogenesis: A green light for cryptochrome research Garry Whitelam Current Biology Volume 5, Issue 12, Pages 1351-1353 (December 1995) DOI: 10.1016/S0960-9822(95)00267-3

Figure 1 . Structural and spectral features of CRY1. The CRY1 protein has domains that show sequence similarity to both microbial photolyase and tropomyosin A. The locations of the putative chromophore-binding sites are indicated, and the green shaded area represents a 40 amino-acid overlap between the photolyase-like and tropomyosin-like domains. Recombinant CRY protein purified from insect cells has an absorption spectrum typical of a flavoprotein. The chromophore released from CRY1 by acid treatment (CRY1-C) has absorption characteristics identical to those of flavin adenine dinucleotide (FAD). Current Biology 1995 5, 1351-1353DOI: (10.1016/S0960-9822(95)00267-3)