2NQT
Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution
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 | C 1 2 1 |
Unit cell lengths | 140.877, 77.983, 87.884 |
Unit cell angles | 90.00, 127.38, 90.00 |
Refinement procedure
Resolution | 40.660 - 1.580 |
R-factor | 0.16422 |
Rwork | 0.163 |
R-free | 0.18531 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.237 |
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 | 1.640 |
High resolution limit [Å] | 1.580 | 1.580 |
Number of reflections | 93633 | |
<I/σ(I)> | 16.87 | 3.34 |
Completeness [%] | 90.3 | 60.2 |
Redundancy | 2.4 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 25% PEG 3350, 0.1M HEPES, 0.2M Ammonium acetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |