4F49
2.25A resolution structure of Transmissible Gastroenteritis Virus Protease containing a covalently bound Dipeptidyl Inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-10-16 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.662, 170.140, 66.130 |
Unit cell angles | 90.00, 113.32, 90.00 |
Refinement procedure
Resolution | 55.708 - 2.250 |
R-factor | 0.1844 |
Rwork | 0.181 |
R-free | 0.24050 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2amp |
RMSD bond length | 0.010 |
RMSD bond angle | 1.305 |
Data reduction software | XDS |
Data scaling software | SCALA (CCP4_3.3.20) |
Phasing software | PHASER (2.4.0) |
Refinement software | PHENIX (dev_961) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 170.140 | 170.140 | 2.370 |
High resolution limit [Å] | 2.250 | 7.120 | 2.250 |
Rmerge | 0.126 | 0.050 | 0.600 |
Total number of observations | 7032 | 28686 | |
Number of reflections | 57334 | ||
<I/σ(I)> | 7.0574 | 16.6 | 1.98 |
Completeness [%] | 98.6 | 99.77 | 97.71 |
Redundancy | 3.56 | 3.72 | 3.48 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 298 | 20% PEG 3350, 100 mM MES, 200 mM sodium acetate, vapor diffusion, temperature 298K |