1B32
OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KMK
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 109.720, 75.720, 70.310 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.750 |
Rwork | 0.182 |
R-free | 0.21400 |
Structure solution method | OTHER |
Starting model (for MR) | 1OLB |
RMSD bond length | 0.010 |
RMSD bond angle | 0.027 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.200 | 1.780 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.059 | 0.203 |
Number of reflections | 60799 | |
<I/σ(I)> | 4 | |
Completeness [%] | 96.7 | 99.2 |
Redundancy | 3.3 |
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) |