1B52
OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KTK
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU |
Spacegroup name | P 21 21 2 A |
Unit cell lengths | 106.351, 76.798, 69.474 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.300 |
Rwork | 0.195 |
R-free | 0.26300 |
Structure solution method | OTHER |
Starting model (for MR) | 1OLB |
RMSD bond length | 0.023 |
RMSD bond angle | 0.051 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.083 * | 0.415 |
Number of reflections | 25448 | |
<I/σ(I)> | 3 | |
Completeness [%] | 98.5 | 90.8 |
Redundancy | 5.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.5 | CO-CRYSTALLIZED WITH URANIUM ACETATE, PH 5.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 5-10 (%(w/v)) | |
3 | 1 | reservoir | sodium acetate | 50 (mM) | |
4 | 1 | reservoir | uranyl acetate | 1 (mM) |