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(inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.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 |
