Philipp Warmer: 2Fo-Fc electron density maps contoured around thymine at position ‘0’ and tryptophan 232 in the ‘−1’ repeat. b: Residues 221 to 239 and residues 256 to 273 each form a helix and an adjoining loop that resembles helix 1 and the RVD loop in the ca

Philipp Warmer — Thu, 03 Jan 2013 10:58:03 GMT

2Fo-Fc electron density maps contoured around thymine at position ‘0’ and tryptophan 232 in the ‘−1’ repeat. b: Residues 221 to 239 and residues 256 to 273 each form a helix and an adjoining loop that resembles helix 1 and the RVD loop in the ca

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== Summary ==
2Fo-Fc electron density maps contoured around thymine at position ‘0’ and tryptophan 232 in the ‘−1’ repeat. b: Residues 221 to 239 and residues 256 to 273 each form a helix and an adjoining loop that resembles helix 1 and the RVD loop in the canonical repeats; the remaining residues in each region are poorly ordered. W232 forms a non polar van der Waals contact with the methyl carbon of the thymine base at position 0.
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Image:Crypticrepeats.jpg - Revision history

Philipp Warmer: 2Fo-Fc electron density maps contoured around thymine at position ‘0’ and tryptophan 232 in the ‘−1’ repeat. b: Residues 221 to 239 and residues 256 to 273 each form a helix and an adjoining loop that resembles helix 1 and the RVD loop in the ca