3TLO
Crystal structure of HCoV-NL63 3C-like protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 90 |
Detector technology | IMAGE PLATE |
Collection date | 2011-01-18 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.144, 83.497, 64.852 |
Unit cell angles | 90.00, 109.20, 90.00 |
Refinement procedure
Resolution | 20.596 - 1.600 |
R-factor | 0.1758 |
Rwork | 0.175 |
R-free | 0.20190 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.032 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 20.600 | 20.600 | 1.690 |
High resolution limit [Å] | 1.600 | 5.060 | 1.600 |
Number of reflections | 82371 | ||
Completeness [%] | 98.3 | 98 | 94.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 289 | 0.1M HEPES, 10% PEG 8000, 5% ethylene glycerol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |