7E6K
Viral protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-07-23 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.979183 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 99.045, 80.681, 52.002 |
Unit cell angles | 90.00, 114.89, 90.00 |
Refinement procedure
Resolution | 24.720 - 1.600 |
R-factor | 0.1717 |
Rwork | 0.170 |
R-free | 0.20180 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6lu7 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 24.720 | 24.720 | 1.640 |
High resolution limit [Å] | 1.600 | 7.150 | 1.600 |
Rmerge | 0.052 | 0.031 | 1.026 |
Rmeas | 0.057 | 0.034 | 1.114 |
Total number of observations | 330594 | ||
Number of reflections | 49021 | 569 | 3583 |
<I/σ(I)> | 18.1 | 43.06 | 2.39 |
Completeness [%] | 99.7 | 96.9 | 99.4 |
Redundancy | 6.744 | 6.016 | 6.656 |
CC(1/2) | 0.999 | 0.999 | 0.849 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 7.5 | 293 | 0.03M Sodium nitrate, 0.03M Sodium phosphate dibasic, 0.03M Ammonium sulfate, 0.1M Sodium HEPES (PH7.5), 0.1M MOPS (PH7.5), 20% PEG 500MME, 10% PEG 20000, protein concentration 5mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 293K |