8PJR
Crystal structure of the SAKe6AC-LB protein
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 | 2022-01-30 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.867023 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 34.730, 47.556, 74.486 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.080 - 1.710 |
| R-factor | 0.1642 |
| Rwork | 0.163 |
| R-free | 0.18250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.056 |
| 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] | 40.080 | 1.740 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Rmerge | 0.068 | 0.189 |
| Rmeas | 0.075 | 0.204 |
| Rpim | 0.030 | 0.075 |
| Total number of observations | 171256 | 9812 |
| Number of reflections | 25559 | 1364 |
| <I/σ(I)> | 18.9 | 11.2 |
| Completeness [%] | 96.9 | |
| Redundancy | 6.7 | 7.2 |
| CC(1/2) | 0.998 | 0.991 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293.15 | 0.2 M Magnesium formate pH 5.9, 20% PEG 3350 |
