1LM1
Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-11-03 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 166.083, 166.083, 219.584 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 129.100 - 2.800 |
| R-factor | 0.23764 |
| Rwork | 0.236 |
| R-free | 0.28700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ea0 |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.230 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.06) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.000 | 2.940 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.120 | 0.455 * |
| Total number of observations | 1595358 * | |
| Number of reflections | 76995 | |
| <I/σ(I)> | 3.8 | 1.7 |
| Completeness [%] | 99.4 | 96.6 |
| Redundancy | 5.7 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 4 * | PEG4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 16 (mg/ml) | |
| 2 | 1 | drop | PIPES-KOH | 25 (mM) | pH7.0 |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | drop | glycerol | 10 (%) | |
| 5 | 1 | reservoir | PEG4000 | 24-30 (%(w/v)) | |
| 6 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.5 |
| 7 | 1 | reservoir | sodium acetate | 200 (mM) |
