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 |