8PJZ
Crystal structure of the computationally designed SAKe6EEtal protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-06-02 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.978560 |
| Spacegroup name | P 1 |
| Unit cell lengths | 34.583, 50.047, 70.787 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.070 - 1.500 |
| R-factor | 0.1713 |
| Rwork | 0.170 |
| R-free | 0.19020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.477 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.870 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.048 | 0.430 |
| Rmeas | 0.059 | 0.527 |
| Rpim | 0.033 | 0.300 |
| Total number of observations | 205437 | 10201 |
| Number of reflections | 71635 | 3476 |
| <I/σ(I)> | 11.1 | 3.1 |
| Completeness [%] | 94.3 | |
| Redundancy | 2.9 | 2.9 |
| CC(1/2) | 0.998 | 0.756 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293.15 | 0.2 M Ammonium acetate, 0.1 M Bis-Tris pH 5.5, 45% (v/v) MPD |
