3MCN
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 | 42.902, 58.190, 105.077 |
| Unit cell angles | 91.00, 80.11, 68.29 |
Refinement procedure
| Resolution | 46.087 - 2.200 |
| R-factor | 0.223 |
| Rwork | 0.220 |
| R-free | 0.28000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB entries 2QX0 1tww |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.134 |
| 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] | 46.100 | 2.279 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.110 | 0.330 |
| Number of reflections | 43569 | |
| <I/σ(I)> | 21.7 | 4.6 |
| Completeness [%] | 93.3 | 76.4 |
| Redundancy | 3.6 | 2.8 |
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 |
