3I3R
X-ray structure dihydrofolate reductase/thymidylate synthase from babesia bovis at 2.35A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 52.540, 83.480, 84.190 |
| Unit cell angles | 119.00, 97.99, 100.69 |
Refinement procedure
| Resolution | 19.690 - 2.350 |
| R-factor | 0.205 |
| Rwork | 0.202 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1QZF modified by the ccp4 program chainsaw |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.191 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 72.200 | 2.410 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.099 | 0.551 |
| Number of reflections | 47995 | |
| <I/σ(I)> | 9.64 | 2.2 |
| Completeness [%] | 96.8 | 96.7 |
| Redundancy | 2.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROFLUDIC MICROBATCH IN A CRYSTAL CARD | 9.5 | 290 | WIZARD SCREEN A1: 20% PEG 8000, 100MM CHES PH 9.5; BABOA.01191.A AT 11.3MG/ML, MICROFLUDIC MICROBATCH IN A CRYSTAL CARD, TEMPERATURE 290K |
