4LNN
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS
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 | 2012-12-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 |
| Unit cell lengths | 109.990, 138.380, 138.740 |
| Unit cell angles | 119.80, 90.19, 93.85 |
Refinement procedure
| Resolution | 84.250 - 3.100 |
| R-factor | 0.217 |
| Rwork | 0.217 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bvc |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 120.000 |
| High resolution limit [Å] | 3.100 |
| Number of reflections | 110080 |
| Completeness [%] | 86.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 40 mg/mL protein, 40% MPD, 200 mM magnesium chloride/sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
