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 |