3NRS
Crystal structure of ligand-free bifunctional folylpolyglutamate synthase/dihydrofolate synthase from yersinia pestis c092
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.628, 83.275, 126.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.800 |
| R-factor | 0.1736 |
| Rwork | 0.173 |
| R-free | 0.19222 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n2a |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.485 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.810 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Rmerge | 0.057 | 0.570 |
| Number of reflections | 63699 | |
| <I/σ(I)> | 30 | 2.5 |
| Completeness [%] | 98.9 | 99.2 |
| Redundancy | 5.2 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 291 | 0.1 M MES, 1.0 M Na/K Tartrate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
