8F09
Crystal structure of a trimethoprim-resistant dihydrofolate reductase (DHFR) enzyme from an uncultured soil bacterium
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2022-04-25 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 36.073, 41.987, 70.380 |
| Unit cell angles | 82.00, 90.00, 72.10 |
Refinement procedure
| Resolution | 34.290 - 2.450 |
| R-factor | 0.2918 |
| Rwork | 0.289 |
| R-free | 0.34930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3jwk |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.611 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | BALBES |
| Refinement software | PHENIX (1.20_4459) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.480 |
| High resolution limit [Å] | 2.440 | 2.440 |
| Rmerge | 0.228 | 0.924 |
| Rpim | 0.162 | 0.635 |
| Number of reflections | 13510 | 651 |
| <I/σ(I)> | 9.1 | 1.65 |
| Completeness [%] | 93.9 | 90.7 |
| Redundancy | 3 | |
| CC(1/2) | 0.974 | 0.398 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 20% ammonium sulfate, 0.1 M Bis-Tris pH 8, cryoprotectant ethylene glycol |
