4GRR
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 |
Wavelength(s) | 1.1 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 95.546, 95.546, 103.879 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.773 - 1.470 |
R-factor | 0.1504 |
Rwork | 0.149 |
R-free | 0.17210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | mif |
RMSD bond length | 0.021 |
RMSD bond angle | 1.779 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.520 |
High resolution limit [Å] | 1.470 | 1.470 |
Rmerge | 0.085 | 0.538 |
Number of reflections | 93378 | |
<I/σ(I)> | 26.7 | 4.53 |
Completeness [%] | 99.9 | 100 |
Redundancy | 11.2 | 10.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 310 | 1.6M ammmonium sualfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K |