3SZG
Crystal structure of C176A glutamine-dependent NAD+ synthetase from M. tuberculosis bound to AMP/PPi and NaAD+
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-14 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 177.940, 177.940, 214.940 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.124 - 2.250 |
| R-factor | 0.1937 |
| Rwork | 0.192 |
| R-free | 0.22940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3dla |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.735 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER (phenix) |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.124 | 2.310 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.187 | 0.823 |
| Number of reflections | 161605 | |
| <I/σ(I)> | 10.8 | 2.84 |
| Completeness [%] | 99.4 | 93.6 |
| Redundancy | 7.9 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 288 | 1.6 M K2HPO4, 100 mM NaH2PO4, EVAPORATION, temperature 288K |
