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 |