7TY1
Crystal structure of apo eosinophil cationic protein (ribonuclease 3) from Macaca fascicularis (MfECP)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08B1-1 |
Synchrotron site | CLSI |
Beamline | 08B1-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-12-10 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.23985 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.330, 39.270, 76.020 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.010 - 1.800 |
R-factor | 0.2109 |
Rwork | 0.207 |
R-free | 0.24980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qmt |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.8.3) |
Refinement software | PHENIX (1.19.1_4122) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 38.020 | 38.020 | 1.860 |
High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
Rmerge | 0.161 | 0.070 | 0.780 |
Rmeas | 0.169 | 0.073 | 0.814 |
Rpim | 0.049 | 0.022 | 0.227 |
Number of reflections | 10862 | 478 | 1076 |
<I/σ(I)> | 14.2 | 29.1 | 3.6 |
Completeness [%] | 100.0 | 100 | 100 |
Redundancy | 12 | 10.3 | 12.8 |
CC(1/2) | 0.998 | 0.998 | 0.900 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 3.5 | 298 | 0.1M Citric acid pH 3.5, 25% PEG 3350 |