Literature summary for 4.1.99.3 extracted from

Mees, A.; Klar, T.; Gnau, P.; Hennecke, U.; Eker, A.P.; Carell, T.; Essen, L.O.
Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair (2004), Science, 306, 1789-1793.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of a DNA photolyase bound to duplex DNA that is bend by 50° and comprises a synthetic cyclobutane pyrimidine dimer lesion. The synthetic cyclobutane pyrimidine dimer lesion is flipped into the active site and split there into two thymines by synchrotron radiation at -173°C. This structure mimics a structural substrate during light-driven DNA repair in which back-flipping of the thymines into duplex DNA has not yet taken place	Synechococcus elongatus PCC 7942 = FACHB-805

Crystallization (Comment)

Organism

crystal structure of a DNA photolyase bound to duplex DNA that is bend by 50° and comprises a synthetic cyclobutane pyrimidine dimer lesion. The synthetic cyclobutane pyrimidine dimer lesion is flipped into the active site and split there into two thymines by synchrotron radiation at -173°C. This structure mimics a structural substrate during light-driven DNA repair in which back-flipping of the thymines into duplex DNA has not yet taken place

Synechococcus elongatus PCC 7942 = FACHB-805

Organism

Organism	UniProt	Comment	Textmining
Synechococcus elongatus PCC 7942 = FACHB-805	-	-	-

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Release 2023.1 (January 2023)