4FRU
Crystal structure of horse wild-type cyclophilin B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-08-12 |
Detector | NOIR-1 |
Wavelength(s) | 0.827 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 64.880, 44.070, 60.570 |
Unit cell angles | 90.00, 95.20, 90.00 |
Refinement procedure
Resolution | 16.416 - 1.100 |
R-factor | 0.1167 |
Rwork | 0.116 |
R-free | 0.13910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cyn |
RMSD bond length | 0.007 |
RMSD bond angle | 1.301 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 16.420 | 1.160 |
High resolution limit [Å] | 1.100 | 1.100 |
Rmerge | 0.078 | 0.272 |
Number of reflections | 62397 | |
<I/σ(I)> | 9.8 | 3.9 |
Completeness [%] | 90.4 | 53.4 |
Redundancy | 3.3 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 295 | 0.1M MES, 10mM ZnCl2, 10% glycerol, 28% PEG MME 550, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K |