1QM7
X-ray structure of a three-fingered chimeric protein, stability of a structural scaffold
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 287 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 58.480, 58.480, 62.310 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
Rwork | 0.202 |
R-free | 0.22100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | FASCICULIN 2 |
RMSD bond length | 0.023 |
RMSD bond angle | 2.866 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.120 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.063 * | 0.335 * |
Number of reflections | 7312 | |
<I/σ(I)> | 22.3 | 2.8 |
Completeness [%] | 97.0 | 41 * |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 4.6 | pH 4.60 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 2 (M) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) |