3M3T
SARS-CoV main protease monomeric Arg298Ala mutant with N-terminal additional residues (Gly-Ser)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-04-03 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0810 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 33.129, 66.210, 64.496 |
Unit cell angles | 90.00, 109.15, 90.00 |
Refinement procedure
Resolution | 33.100 - 2.900 |
Rwork | 0.185 |
R-free | 0.27320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB code 2H2Z |
RMSD bond length | 0.005 |
RMSD bond angle | 1.102 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASES |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.090 | 0.285 |
Number of reflections | 6356 | |
<I/σ(I)> | 21.1 | 1.1 |
Completeness [%] | 95.7 | 68.8 |
Redundancy | 6.1 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 2% PEG 6000, 0.1M Mes , pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |