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

2013-01-03T10:58:03Z

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

New page

== 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.
== Licensing ==
{{subst:No license from license selector|Don't know}}

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