3D84
Structural Analysis of a Holo Enzyme Complex of Mouse Dihydrofolate Reductase with NADPH and a Ternary Complex with the Potent and Selective Inhibitor 2.4-Diamino-6-(-2'-hydroxydibenz[b,f]azepin-5-yl)methylpteridine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-12-03 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.226, 61.172, 43.150 |
| Unit cell angles | 90.00, 118.26, 90.00 |
Refinement procedure
| Resolution | 23.830 - 1.900 |
| R-factor | 0.18902 |
| Rwork | 0.187 |
| R-free | 0.22890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fzj |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.063 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.010 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.034 | 0.076 |
| Number of reflections | 13551 | |
| <I/σ(I)> | 0.033 | 0.9 |
| Completeness [%] | 90.7 | 50.5 |
| Redundancy | 9.5 | 14 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 298 | 10 mM Hepes, pH 7.4, 17 mM Na acetate, pH 6.5, 85 mM Tris HCl, 25% PEG 4K, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
