4LNF
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-Q
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 | 2012-12-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 112.000, 137.500, 137.700 |
| Unit cell angles | 119.80, 90.30, 93.40 |
Refinement procedure
| Resolution | 119.014 - 2.949 |
| R-factor | 0.195 |
| Rwork | 0.194 |
| R-free | 0.25870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4lnn |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.124 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 119.014 | 3.110 |
| High resolution limit [Å] | 2.949 | 2.949 |
| Number of reflections | 143849 | |
| <I/σ(I)> | 7 | 2 |
| Completeness [%] | 95.9 | 96.2 |
| Redundancy | 1.9 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 40% MPD, 0.2 M magnesium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
