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 |