8T19
RiPP precursor peptide recognition element (RRE) domain of Ocin-ThiF-like partner protein, PbtF, bound to an 8 residue fragment of its precursor peptide, PbtA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-03-10 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 40.259, 40.259, 101.839 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.990 - 1.230 |
| R-factor | 0.223 |
| Rwork | 0.221 |
| R-free | 0.25580 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.897 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | AutoSol |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.990 | 1.274 |
| High resolution limit [Å] | 1.230 | 1.230 |
| Rmerge | 0.012 | 0.232 |
| Rmeas | 0.017 | 0.329 |
| Rpim | 0.012 | 0.232 |
| Number of reflections | 28683 | 2805 |
| <I/σ(I)> | 24.06 | 2.75 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 2 | 2 |
| CC(1/2) | 1.000 | 0.881 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 27.5% PEG 3350, 0.2 M MgCl2, 0.1 M tris pH 8.0 |
