7LSC
Crystal structure of near-infrared fluorescent protein miRFP670nano3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-02-15 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 111.531, 73.953, 83.743 |
Unit cell angles | 90.00, 101.71, 90.00 |
Refinement procedure
Resolution | 29.830 - 1.800 |
R-factor | 0.1789 |
Rwork | 0.178 |
R-free | 0.23710 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6mgh |
RMSD bond length | 0.010 |
RMSD bond angle | 2.283 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 1.860 |
High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
Rmerge | 0.074 | 0.052 | 0.815 |
Rmeas | 0.083 | 0.059 | 0.935 |
Rpim | 0.037 | 0.027 | 0.446 |
Total number of observations | 274220 | ||
Number of reflections | 60575 | 6164 | 5734 |
<I/σ(I)> | 9.8 | ||
Completeness [%] | 98.5 | 98.1 | 93.6 |
Redundancy | 4.5 | 4.5 | 3.9 |
CC(1/2) | 0.994 | 0.682 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 293 | 8.4% PEG4000, 3.6% MPD, 0.06 M sodium/potassium phosphate, pH 6.3 |