7MYL
Crystal structure of DfrA1 dihydrofolate reductase in complex with TRIMETHOPRIM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-1 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-11-24 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.9201 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.072, 72.890, 125.122 |
| Unit cell angles | 90.00, 90.56, 90.00 |
Refinement procedure
| Resolution | 63.060 - 2.150 |
| R-factor | 0.2173 |
| Rwork | 0.215 |
| R-free | 0.26590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ecc |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.414 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 72.890 | 2.210 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.190 | 0.905 |
| Rmeas | 0.206 | 0.983 |
| Rpim | 0.078 | 0.379 |
| Number of reflections | 53224 | 4327 |
| <I/σ(I)> | 7.6 | 1.9 |
| Completeness [%] | 98.6 | 97.8 |
| Redundancy | 6.8 | 6.6 |
| CC(1/2) | 0.993 | 0.558 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277.15 | 22% PEG3350, 0.1M Na-Cacodylate pH 6.5, 0.36M MgCl2 and 2 mM DTT |
