9DAQ
Structure of E. coli dihydrofolate reductase (DHFR) in an occluded conformation and in complex with a cycloguanil derivative
This is a non-PDB format compatible entry.
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 | 67.032, 67.032, 216.062 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 34.660 - 2.350 |
| R-factor | 0.2366 |
| Rwork | 0.236 |
| R-free | 0.25540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.508 |
| 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] | 34.700 | 2.590 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rpim | 0.033 | 0.445 |
| Number of reflections | 8096 | 406 |
| <I/σ(I)> | 14.2 | 1.7 |
| Completeness [%] | 94.2 | 81.5 |
| Redundancy | 22.6 | 22 |
| CC(1/2) | 0.998 | 0.802 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 277 | 2.0 M ammonium sulfate, 0.1 M sodium acetate |
