6GWI
The crystal structure of Halomonas elongata amino-transferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-11-11 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 1 |
Spacegroup name | P 1 |
Unit cell lengths | 56.344, 61.875, 67.475 |
Unit cell angles | 83.45, 82.58, 72.52 |
Refinement procedure
Resolution | 46.915 - 2.000 |
R-factor | 0.1622 |
Rwork | 0.160 |
R-free | 0.21000 |
Data reduction software | X-Area |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.920 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.104 | 0.429 |
Rmeas | 0.147 | |
Rpim | 0.104 | 0.429 |
Number of reflections | 54196 | 3885 |
<I/σ(I)> | 8.5 | 2.4 |
Completeness [%] | 93.4 | 90.7 |
Redundancy | 1.7 | 1.6 |
CC(1/2) | 0.997 | 0.831 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.9 | 293 | Hampton Research PEG/ION screen condition 25 (20% PEG3350, 0.2M magnesium acetate, pH 7.9). |