3S9U
Bacillus anthracis Dihydrofolate Reductase bound to propargyl-linked TMP analog, UCP120J
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 | 2008-08-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979505 |
| Spacegroup name | P 42 |
| Unit cell lengths | 78.187, 78.187, 67.094 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.800 - 1.900 |
| R-factor | 0.19161 |
| Rwork | 0.190 |
| R-free | 0.22311 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3e0b |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.131 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.830 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.073 | 0.397 |
| Number of reflections | 30364 | |
| <I/σ(I)> | 25.6 | 3.5 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 7.4 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 300 | initial hits were grown at room temperature by hanging drop diffusion in 21.0% (w/v) PEG 10,000, 0.1 M MES, pH 6.75, at an equal ratio of protein to crystallization solution. Microseeding was used to obtain isolated crystals in 11% PEG 10,000 and 0.1 MES, pH 6.75 at a protein concentration of 8 mg/mL, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
