3BXX
Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of the catalytic site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-03-17 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9330 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 174.943, 174.943, 290.167 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 75.810 - 2.900 |
| R-factor | 0.292 |
| Rwork | 0.288 |
| R-free | 0.36600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.331 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 75.810 | 75.810 | 3.060 |
| High resolution limit [Å] | 2.900 | 9.170 | 2.900 |
| Rmerge | 0.153 | 0.061 | 0.425 |
| Total number of observations | 25055 | 119891 | |
| Number of reflections | 58753 | ||
| <I/σ(I)> | 4.1 | 5.7 | 1.7 |
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 14.3 | 11.9 | 14.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.9 | 293 | NaCl 130 mM, 35% PEG 3350, 100 mM Hepes pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
