4LNK
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex
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 | 2012-12-23 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 138.500, 240.860, 207.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 120.065 - 2.870 |
| R-factor | 0.1999 |
| Rwork | 0.195 |
| R-free | 0.23560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4lnn |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.327 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 120.070 | 3.030 |
| High resolution limit [Å] | 2.870 | 2.870 |
| Number of reflections | 72956 | |
| <I/σ(I)> | 6 | 1.7 |
| Completeness [%] | 91.0 | 69.8 |
| Redundancy | 3.3 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.8 | 298 | 10% PEG, 15 mM magnesium chloride, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
