1GS5
N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate N-acetylglutamate and its substrate analog AMPPNP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-05-15 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.564, 72.332, 107.418 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 53.710 * - 1.500 |
R-factor | 0.2088 * |
Rwork | 0.209 |
R-free | 0.21280 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gsj |
RMSD bond length | 0.012 * |
RMSD bond angle | 2.080 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 53.710 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.042 * | 0.349 * |
Total number of observations | 196777 * | |
Number of reflections | 37500 * | |
<I/σ(I)> | 9.2 | 2.1 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 5.2 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 27-32% PEG MONOMETHYLETHER 2000, 0.1-0.3M AMMONIUM SULFATE, 5% ETHYLENE GLYCOL, 0.1M SODIUM ACETATE PH 4.6 |