EC Number   |
|---|
   1.21.3.3 | crystal structure of the H174A variant shows significant structural rearrangements compared to wild-type enzyme. Residue H174 is part of a hydrogen bonding network that stabilizes the negative charge at the N1/C2=O locus via interaction with the hydroxyl group at C2 of the ribityl side chain of the flavin cofactor |
| 1.21.3.3 | hanging drop vapor diffusion method, using 0.2 M sodium thiocyanate and 20% (w/v) PEG 3350 |
| 1.21.3.3 | microbatch method, using 0.1 M HEPES buffer pH 7.0 containing 30% (v/v) Jeffamine ED 2001, pH 7.0 |
| 1.21.3.3 | the crystal structure of Berberine bridge enzyme in complex with dehydroscoulerine is determined to 1.63 A resolution |
| 1.21.3.3 | the crystal structures of berberine bridge enzyme in two different crystal forms, monoclinic and tetragonal, and in complex with (S)-reticuline are determined |
| 1.21.3.3 | the crystal structures of the mutants H104A, C166A, C166A in complex with (S)-reticuline and of the wild-type enzyme in complex with (S)-scoulerine are determined |
