7NCE
Glutathione-S-transferase GliG mutant N27A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-03-14 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.190, 85.370, 345.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.1924 |
Rwork | 0.191 |
R-free | 0.22420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7nc3 |
RMSD bond length | 0.002 |
RMSD bond angle | 1.158 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.059 | 0.562 |
Number of reflections | 106999 | 14562 |
<I/σ(I)> | 12.6 | 2.5 |
Completeness [%] | 97.6 | |
Redundancy | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.2 M ammonium acetate, 0.1 M bis-tris pH 5.5, 24 % PEG3350 |