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 |