6OFL
Crystal structure of green fluorescent protein (GFP); S65T, Y66(3-ClY); ih circular permutant (50-51)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL14-1 |
Synchrotron site | SSRL |
Beamline | BL14-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-10-27 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.220, 68.730, 60.880 |
Unit cell angles | 90.00, 100.57, 90.00 |
Refinement procedure
Resolution | 36.520 - 1.250 |
R-factor | 0.12834 |
Rwork | 0.127 |
R-free | 0.15837 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zf3 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.616 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.520 | 1.280 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmeas | 0.058 | 1.650 |
Number of reflections | 113139 | 7995 |
<I/σ(I)> | 27.4 | 1.5 |
Completeness [%] | 96.9 | 93.6 |
Redundancy | 23 | 10.9 |
CC(1/2) | 1.000 | 0.721 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.15 M ammonium acetate, 30% PEG 3350 |