6JC8
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Glu
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-14 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.9785 |
Spacegroup name | P 1 |
Unit cell lengths | 84.090, 83.930, 88.459 |
Unit cell angles | 106.60, 109.11, 95.13 |
Refinement procedure
Resolution | 49.460 - 2.250 |
R-factor | 0.1788 |
Rwork | 0.177 |
R-free | 0.21460 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5dds |
RMSD bond length | 0.009 |
RMSD bond angle | 1.584 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless (0.5.21) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 49.460 | 49.460 | 2.290 |
High resolution limit [Å] | 2.250 | 12.320 | 2.250 |
Rmerge | 0.122 | 0.058 | 0.628 |
Rmeas | 0.141 | 0.067 | 0.728 |
Rpim | 0.071 | 0.035 | 0.368 |
Total number of observations | 380457 | 2229 | 18981 |
Number of reflections | 96761 | 599 | 4822 |
<I/σ(I)> | 8.6 | 19.9 | 2.3 |
Completeness [%] | 95.0 | 96.8 | 95.5 |
Redundancy | 3.9 | 3.7 | 3.9 |
CC(1/2) | 0.992 | 0.992 | 0.772 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 293 | 0.2M Sodium acetate, 0.1M TRIS pH 8.5, 32% PEG 3350, 2% glycerol |