6X5W
Peptide-bound structure of Marinomonas primoryensis peptide-binding domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2019-09-26 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 1 |
| Unit cell lengths | 51.163, 58.922, 63.249 |
| Unit cell angles | 62.51, 85.81, 65.93 |
Refinement procedure
| Resolution | 55.540 - 1.800 |
| R-factor | 0.1921 |
| Rwork | 0.190 |
| R-free | 0.22810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5k8g |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.828 |
| Data reduction software | DIALS |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.540 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.146 | 0.809 |
| Number of reflections | 138852 | 51767 |
| <I/σ(I)> | 16.22 | |
| Completeness [%] | 97.7 | 94.4 |
| Redundancy | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 4.6 | 293 | ~0.1 M calcium chloride, ~0.1 M sodium acetate (pH 4.6), ~30% (w/v) PEG 400 |
