1QKA
OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KRK
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Detector | R-AXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 109.926, 75.446, 70.061 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.800 |
R-factor | 0.168 * |
Rwork | 0.176 |
R-free | 0.22194 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1OLB |
RMSD bond length | 0.010 |
RMSD bond angle | 0.026 |
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 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.097 | 0.309 |
Number of reflections | 52404 | |
<I/σ(I)> | 5.6 | 1.2 |
Completeness [%] | 95.2 | 72.4 |
Redundancy | 5.6 | 2.4 |
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 | PEG4000 | 5-10 (%(w/v)) | |
2 | 1 | drop | sodium acetate | 50 (mM) | |
3 | 1 | drop | uranyl acetate | 1 (mM) | |
4 | 1 | drop | peptide | 30 (mg/ml) |