1MFF
MACROPHAGE MIGRATION INHIBITORY FACTOR Y95F MUTANT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1998-09 |
Detector | RIGAKU |
Spacegroup name | P 63 |
Unit cell lengths | 96.160, 96.160, 88.520 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 33.000 - 2.000 |
R-factor | 0.191 |
Rwork | 0.191 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mfi |
RMSD bond length | 0.013 |
RMSD bond angle | 27.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.068 * | 0.390 * |
Total number of observations | 195439 * | |
Number of reflections | 30194 | |
<I/σ(I)> | 12.1 | 3.7 |
Completeness [%] | 95.9 | 88.5 |
Redundancy | 4.3 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.4 * | 22 * | pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 20 (mM) | ||
4 | 1 | reservoir | PEG8000 | 25 (%) | |
5 | 1 | reservoir | sodium phosphate | 42 (mM) |