4X2Y
Crystal structure of a chimeric Murine Norovirus NS6 protease (inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-04-23 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54 |
Spacegroup name | P 1 |
Unit cell lengths | 35.520, 47.320, 53.070 |
Unit cell angles | 104.45, 91.53, 110.61 |
Refinement procedure
Resolution | 19.273 - 2.417 |
R-factor | 0.2129 |
Rwork | 0.210 |
R-free | 0.26160 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ash |
RMSD bond length | 0.003 |
RMSD bond angle | 0.673 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.273 | 2.503 |
High resolution limit [Å] | 2.417 | 2.417 |
Rmerge | 0.093 | 0.271 |
Number of reflections | 10817 | |
<I/σ(I)> | 6.7 | 2.31 |
Completeness [%] | 91.1 | 66.47 |
Redundancy | 1.8 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | 0.2 M KSCN, 0.1 M Bis-Tris propane pH 6.5-7.5, 20% w/v PEG 3350, cryo 30% (v/v) PEG 3350 |