1A40
PHOSPHATE-BINDING PROTEIN WITH ALA 197 REPLACED WITH TRP
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-05 |
Detector | MACSCIENCE |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.410, 62.760, 122.730 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.700 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2abh |
RMSD bond length | 0.013 |
RMSD bond angle | 23.780 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.85) |
Refinement software | X-PLOR (3.85) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.780 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.086 * | 0.314 * |
Number of reflections | 35260 | |
<I/σ(I)> | 8 | 4 |
Completeness [%] | 92.3 | 63.6 |
Redundancy | 6 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 | pH 4.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5.5 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 15 (mM) | |
3 | 1 | reservoir | PEG6000 | 20 (%(w/v)) | |
4 | 1 | reservoir | 50 (mM) | ||
5 | 1 | reservoir | potassium phosphate | 2 (mM) | |
6 | 1 | reservoir | potassium acetate | 20 (mM) |