8FRE
Designed loop protein RBL4
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-11-08 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 62.287, 215.442, 28.008 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 59.840 - 1.800 |
| R-factor | 0.2363 |
| Rwork | 0.234 |
| R-free | 0.28070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.060 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.1_4122) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.840 | 1.864 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmeas | 0.150 | 3.557 |
| Rpim | 0.057 | 1.298 |
| Number of reflections | 35977 | 3521 |
| <I/σ(I)> | 5.7 | 0.36 |
| Completeness [%] | 98.7 | 96.09 |
| Redundancy | 7.2 | 7.2 |
| CC(1/2) | 0.989 | 0.335 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.4 | 293 | 100 mM sodium acetate, pH 4.4, 2% PEG4000 |
