5Z33
Crystal structure of Mitogen-activated Protein Kinase Mps1 in Magnaporthe oryzae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-10-31 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9792 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 74.549, 74.549, 158.561 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 59.795 - 1.990 |
R-factor | 0.1886 |
Rwork | 0.187 |
R-free | 0.22170 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.048 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AutoSol |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 79.280 | 2.100 |
High resolution limit [Å] | 1.990 | 1.990 |
Number of reflections | 379824 | |
<I/σ(I)> | 12.8 | |
Completeness [%] | 99.9 | |
Redundancy | 10.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | Sodium cacodylate trihydrate, tacsimate, spermine |