8BFR
The E. coli TrpD2 protein YbiB at 1.3 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-11-07 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97856 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 134.154, 64.004, 47.496 |
Unit cell angles | 90.00, 97.22, 90.00 |
Refinement procedure
Resolution | 66.550 - 1.300 |
R-factor | 0.1366 |
Rwork | 0.135 |
R-free | 0.16670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4muo |
RMSD bond length | 0.009 |
RMSD bond angle | 1.087 |
Data reduction software | autoPROC (1.0.5) |
Data scaling software | autoPROC (1.0.5) |
Phasing software | PHENIX (1.20.1_4487) |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 66.550 | 1.397 |
High resolution limit [Å] | 1.300 | 1.300 |
Number of reflections | 80496 | 4026 |
<I/σ(I)> | 10.8 | |
Completeness [%] | 93.6 | |
Redundancy | 6.8 | |
CC(1/2) | 0.998 | 0.624 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.1 M MES pH 6.2, 15 % w/v PEG 3350 |