2PQ2
Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2007-02-10 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 68.314, 68.314, 108.418 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 57.300 - 1.820 |
R-factor | 0.17016 |
Rwork | 0.168 |
R-free | 0.20728 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dp4 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.224 |
Data reduction software | AUTOMAR |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.300 | 1.870 |
High resolution limit [Å] | 1.820 | 1.820 |
Number of reflections | 23699 | |
<I/σ(I)> | 12.2 | 2 |
Completeness [%] | 99.6 | 97.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 0.2M AMMONIUM ACTATE, 0.1M SODIUM ACETATE, 30% PEG 4000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |