Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Collection date | 1997-11-30 |
Detector | SIEMENS |
Spacegroup name | H 3 2 |
Unit cell lengths | 91.440, 91.440, 107.750 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 2.700 |
Rwork | 0.242 |
R-free | 0.27800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tfg |
RMSD bond length | 0.007 |
RMSD bond angle | 23.500 * |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | AMoRE |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.041 | 0.123 |
Number of reflections | 4647 | |
<I/σ(I)> | 24.2 | 5.4 |
Completeness [%] | 94.6 | 82.2 |
Redundancy | 3 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.4 | 20 * | CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 100 MM LITHIUM SULFATE, 12% TERT-BUTANOL, 50 MM CITRATE, PH 5.4 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | acetate | 20 (mM) | |
3 | 1 | reservoir | citrate | 50 (mM) | |
4 | 1 | reservoir | lithium sulfate | 100 (mM) | |
5 | 1 | reservoir | tertbutanol | 12 (%(v/v)) |