2HE9
Structure of the peptidylprolyl isomerase domain of the human NK-tumour recognition protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-06-10 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 64.753, 72.786, 73.014 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.910 - 2.000 |
R-factor | 0.14889 |
Rwork | 0.146 |
R-free | 0.19752 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ZCX |
RMSD bond length | 0.017 |
RMSD bond angle | 1.515 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 23807 | |
<I/σ(I)> | 15.2 | |
Completeness [%] | 99.9 | 98.7 |
Redundancy | 7 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | Well solution: 21% Peg 3350, 0.25M potassium sulfate; Protein solution: 50 mM Tris pH 7.5, 100 mM NaCl, 1 mM DTT, 15 mg/mL protein, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |