6VFM
Crystal structure of SpeG allosteric polyamine acetyltransferase from Bacillus thuringiensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-09-06 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 159.374, 159.374, 106.205 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 63.740 - 2.670 |
| R-factor | 0.2753 |
| Rwork | 0.274 |
| R-free | 0.29310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wr7 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.643 |
| Data reduction software | HKL-2000 |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 63.740 | 63.740 | 2.800 |
| High resolution limit [Å] | 2.670 | 8.860 | 2.670 |
| Rmerge | 0.318 | 0.077 | 1.499 |
| Rmeas | 0.325 | 0.079 | 1.529 |
| Rpim | 0.065 | 0.017 | 0.297 |
| Total number of observations | 589520 | 16297 | 81259 |
| Number of reflections | 23127 | 738 | 3001 |
| <I/σ(I)> | 8.1 | 15.9 | 3.2 |
| Completeness [%] | 100.0 | 99.7 | 100 |
| Redundancy | 25.5 | 22.1 | 27.1 |
| CC(1/2) | 0.998 | 0.999 | 0.734 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | TRIS pH7.5, PEG4000, and 0.2 M Lithium sulfate |
