3MCM
Crystal Structure of the 6-hyroxymethyl-7,8-dihydropterin pyrophosphokinase dihydropteroate synthase bifunctional enzyme from Francisella tularensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 42.821, 57.779, 105.127 |
| Unit cell angles | 91.13, 99.39, 111.64 |
Refinement procedure
| Resolution | 38.442 - 2.200 |
| R-factor | 0.219 |
| Rwork | 0.215 |
| R-free | 0.27800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB entries 2QX0 1tww |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.127 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.5_2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.600 | 2.278 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.130 | 0.280 |
| Number of reflections | 44140 | |
| <I/σ(I)> | 23.6 | 5.3 |
| Completeness [%] | 94.4 | 80.1 |
| Redundancy | 3.5 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 291 | TRIS, Na Acetate, PEG 4000, Glyerol, pH 8.0, vapor diffusion, sitting drop, temperature 291K |
