3FQO
Staphylococcus aureus F98Y mutant dihydrofolate reductase complexed with NADPH and 2,4-diamino-5-[3-(2,5-dimethoxyphenyl)prop-1-ynyl]-6-ethylpyrimidine (UCP120B)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 77.2 |
| Detector technology | CCD |
| Collection date | 2008-04-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.080900 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 78.866, 78.866, 107.825 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.330 - 2.090 |
| R-factor | 0.218 |
| Rwork | 0.216 |
| R-free | 0.26100 |
| Structure solution method | DIFFERENCE FOURIER |
| Starting model (for MR) | Sa F98Y DHFR bound to Folate and NADPH (Dale et al. J.Mol.Biol. 1997 structure not deposited in the PDB) |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.395 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.330 | 2.180 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Rmerge | 0.064 | 0.406 |
| Number of reflections | 11685 | |
| <I/σ(I)> | 5 | 3.8 |
| Completeness [%] | 99.1 | 100 |
| Redundancy | 9.4 | 9.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 15% PEG 10000, 150mM Sodium acetate, 100mM MES pH 6.5, 5% Butyrlactone, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
