4LNI
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state 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 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 |
Unit cell lengths | 110.200, 141.600, 142.100 |
Unit cell angles | 60.29, 67.38, 76.20 |
Refinement procedure
Resolution | 117.103 - 2.579 |
R-factor | 0.1655 |
Rwork | 0.165 |
R-free | 0.22310 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 2.184 |
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] | 117.103 | 2.720 |
High resolution limit [Å] | 2.579 | 2.579 |
Number of reflections | 196618 | |
<I/σ(I)> | 3.5 | 3.5 |
Completeness [%] | 90.9 | 67 |
Redundancy | 2 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 5% PEG8000, 0.025 mM magnesium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |