3SEQ
Crystal structure of C176A mutant of glutamine-dependent NAD+ synthetase from M. tuberculosis in complex with AMPCPP and NaAD+
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-24 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.98 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 178.166, 178.166, 214.907 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.091 - 2.734 |
R-factor | 0.1652 |
Rwork | 0.163 |
R-free | 0.21240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3dla |
RMSD bond length | 0.012 |
RMSD bond angle | 1.470 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER (phenix) |
Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.850 |
High resolution limit [Å] | 2.734 | 2.734 |
Number of reflections | 88274 | |
<I/σ(I)> | 15.6 | 3.7 |
Completeness [%] | 96.6 | 91.2 |
Redundancy | 14.5 | 8.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 8 | 288 | 1.4 M ammonium citrate tribasic dihydrate, 7.5 % glycerol, pH 8.0, EVAPORATION, temperature 288K |