4GRP
Crystallographic and biological characterization of N- and C- terminus mutants of human MIF
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-12-10 |
Detector | PSI PILATUS 6M |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 50.050, 76.250, 82.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.840 - 1.270 |
R-factor | 0.138 |
Rwork | 0.137 |
R-free | 0.16900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MIF |
RMSD bond length | 0.014 |
RMSD bond angle | 1.484 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.730 | 1.700 |
High resolution limit [Å] | 1.270 | 1.340 |
Rmerge | 0.090 | |
Number of reflections | 81548 | |
<I/σ(I)> | 10.8 | 1.8 |
Completeness [%] | 97.6 | 48.8 |
Redundancy | 8.2 | 0.46 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.6 | 293 | 1.6M ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |