2I3G
Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis in complex with NADP+.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-14 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.11587 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 141.456, 78.214, 88.034 |
Unit cell angles | 90.00, 127.46, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.850 |
R-factor | 0.16336 |
Rwork | 0.161 |
R-free | 0.20498 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vkn |
RMSD bond length | 0.014 |
RMSD bond angle | 1.495 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Number of reflections | 59626 | |
Completeness [%] | 91.3 | 88.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 295 | 17% PEG 10000, 0.1 M Bis-Tris pH 5.5, 0.1 M Ammonium Acetate, VAPOR DIFFUSION, SITTING DROP, temperature 295K |