3MJZ
The crystal structure of native FG41 MSAD
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-06-22 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 88.955, 94.692, 190.701 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.020 - 2.400 |
R-factor | 0.204 |
Rwork | 0.200 |
R-free | 0.27900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2aal |
RMSD bond length | 0.013 |
RMSD bond angle | 1.493 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CaspR |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 42.020 | 50.000 | 2.090 |
High resolution limit [Å] | 2.020 | 4.350 | 2.020 |
Rmerge | 0.154 | 0.063 | 0.673 |
Number of reflections | 54052 | ||
<I/σ(I)> | 6.9 | ||
Completeness [%] | 85.7 | 99.8 | 86.7 |
Redundancy | 9 | 9.6 | 9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Sitting drop | 7.5 | 277 | 3 micro liter of protein solution (20.5 mg/mL in 10 mM sodium phosphate buffer, pH 8.0) mixed with 3 micro liter crystallization solution (0.1 M HEPES-Na buffer, pH 7.5, 2% v/v polyethylene glycol 400, 2.0 M ammonium sulfate), Sitting drop, temperature 277K |