2I3A
Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis
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 | 2006-04-13 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.11587 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 89.695, 104.031, 138.435 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.680 - 2.150 |
R-factor | 0.16429 |
Rwork | 0.161 |
R-free | 0.22450 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 1.798 |
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 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Number of reflections | 69868 | |
Completeness [%] | 98.9 | 92.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | 20% PEG MME 5000, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |