3TQV
Structure of the nicotinate-nucleotide pyrophosphorylase from Francisella tularensis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4C |
| Synchrotron site | NSLS |
| Beamline | X4C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-13 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.780, 46.474, 99.814 |
| Unit cell angles | 90.00, 108.26, 90.00 |
Refinement procedure
| Resolution | 24.258 - 2.620 |
| R-factor | 0.2202 |
| Rwork | 0.217 |
| R-free | 0.27890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.141 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.550 |
| High resolution limit [Å] | 2.510 | 6.810 | 2.510 |
| Rmerge | 0.108 | 0.045 | 0.368 |
| Number of reflections | 21851 | ||
| <I/σ(I)> | 9.2 | ||
| Completeness [%] | 96.6 | 96 | 80.2 |
| Redundancy | 2.9 | 3.1 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | sitting drop | 7.5 | 293 | 200 mM Ammonium Sulfate, 20% PEG 3350, pH 7.5, sitting drop, temperature 293K |
