3K2H
Co-crystal structure of dihydrofolate reductase/thymidylate synthase from Babesia bovis with dUMP, Pemetrexed and NADP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-09-11 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 51.144, 83.196, 83.378 |
| Unit cell angles | 119.69, 90.85, 101.71 |
Refinement procedure
| Resolution | 35.200 - 2.200 |
| R-factor | 0.192 |
| Rwork | 0.190 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3i3r |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.507 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.096 | 0.286 |
| Number of reflections | 58064 | |
| <I/σ(I)> | 15.4 | 3.16 |
| Completeness [%] | 98.5 | 82.6 |
| Redundancy | 4 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 289 | 11.3 mg/mL BaboA.01191.a, 2 mM dUMP, 2 mM Pemetrexed, NADP carried through from protein purification so it could be NADP or NADPH; soak of apo crystals grown in 20% PEG 8000, 0.1 M CHES pH 9.5; crystal tracking ID 204850f1, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
