3L07
Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative bifunctional protein folD from Francisella tularensis.
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 | 2009-11-30 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.299, 73.385, 106.916 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.200 - 1.880 |
| R-factor | 0.168 |
| Rwork | 0.165 |
| R-free | 0.20800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a4i |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.663 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.200 | 1.910 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.089 | 0.805 |
| Number of reflections | 45729 | |
| <I/σ(I)> | 9.4 | 2.78 |
| Completeness [%] | 99.8 | 98.1 |
| Redundancy | 7.2 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.2 M ammonium acetate, 0.1 M HEPES buffre, 25% PEG-3350, 10 mM NADP, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
