Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.720, 108.980, 90.360 |
Unit cell angles | 90.00, 95.57, 90.00 |
Refinement procedure
Resolution | 8.000 * - 2.500 |
R-factor | 0.209 |
Rwork | 0.209 |
R-free | 0.26500 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fnd poly-Ala |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.600 * |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.580 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.094 | 0.319 |
Total number of observations | 61664 * | |
Number of reflections | 26895 | |
Completeness [%] | 83.9 | 83.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8 * | 20 * | TRIS/HCL, AMMONIUM SULFATE, VAPOR DIFFUSION |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
2 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
3 | 1 | drop | protein | 15.0 (mg/ml) | |
4 | 1 | drop | Tris-HCl | 20 (mM) | pH8.0 |