2PBC
FK506-binding protein 2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-06-23 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.430, 39.335, 108.316 |
Unit cell angles | 90.00, 91.28, 90.00 |
Refinement procedure
Resolution | 23.060 - 1.800 |
R-factor | 0.18861 |
Rwork | 0.185 |
R-free | 0.25986 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y0o |
RMSD bond length | 0.019 |
RMSD bond angle | 1.687 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.100 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 32970 | |
<I/σ(I)> | 27.8 | 7.8 |
Completeness [%] | 98.5 | 85.3 |
Redundancy | 3.4 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 32% PEG MME550, CRYOPROTECTED IN PARATONE-N, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |