9DAR
Structure of E. coli dihydrofolate reductase (DHFR) in an occluded conformation and in complex with cycloguanil
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 | 2024-04-07 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.920 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 68.076, 68.076, 212.602 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 34.490 - 2.170 |
| R-factor | 0.2116 |
| Rwork | 0.210 |
| R-free | 0.25190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.292 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.18.2_3874: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.500 | 2.380 |
| High resolution limit [Å] | 2.170 | 2.170 |
| Rpim | 0.025 | 0.438 |
| Number of reflections | 12722 | 636 |
| <I/σ(I)> | 16.6 | 1.6 |
| Completeness [%] | 94.2 | 56.3 |
| Redundancy | 23 | 19.9 |
| CC(1/2) | 0.999 | 0.768 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 0.2 M ammonium citrate dibasic, 20% (w/v) PEG 3350 |
