3Q3X
Crystal structure of the main protease (3C) from human enterovirus B EV93
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-04 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.872600 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.072, 65.216, 66.355 |
Unit cell angles | 90.00, 90.67, 90.00 |
Refinement procedure
Resolution | 46.524 - 1.900 |
R-factor | 0.1514 |
Rwork | 0.148 |
R-free | 0.21010 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1l1n |
RMSD bond length | 0.012 |
RMSD bond angle | 1.401 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.2.19) |
Phasing software | PHASER (1.3) |
Refinement software | REFMAC (refmac_5.5.0066) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 66.370 | 46.524 | 2.000 |
High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
Rmerge | 0.127 | 0.048 | 0.412 |
Total number of observations | 4304 | 11837 | |
Number of reflections | 26356 | ||
<I/σ(I)> | 8.7 | 12.4 | 1.6 |
Completeness [%] | 99.9 | 98.5 | 100 |
Redundancy | 4.4 | 5 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 18% PEG 8K, 0.1M cacodylate, 0.2M magnesium acetate, cryo + 20% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |