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. 2009 Apr 28;7(4):e1000094. doi: 10.1371/journal.pbio.1000094

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© 2009 Hennig et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Ribbon presentation of the dPER[232–599] dimer with molecule 1 shown in cyan, molecule 2 in grey. The inset shows a close-up view highlighting residues Trp482 and Met560, which have been mutated in this study. The per ^L mutation site (Val243) is also highlighted.

(B) Stereo view of the dPERΔαF[232–538] monomer structure.

(C) Superposition of the dPERΔαF[232–538] monomer structure (green) on molecule 1 (cyan) and 2 (grey) of the dPER[232–599] dimer. The two orientations are related by 180 ° rotations.