4YUH
Multiconformer synchrotron model of CypA at 150 K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 150 |
Detector technology | CCD |
Collection date | 2012-03-04 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9767 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 42.450, 51.820, 88.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.117 - 1.340 |
R-factor | 0.1254 |
Rwork | 0.124 |
R-free | 0.15610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cpl |
RMSD bond length | 0.008 |
RMSD bond angle | 1.198 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.117 | 1.390 |
High resolution limit [Å] | 1.340 | 1.340 |
Rmerge | 0.030 | 0.294 |
Number of reflections | 42288 | |
<I/σ(I)> | 25.95 | 3.24 |
Completeness [%] | 95.0 | 80 |
Redundancy | 3.8 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | Crystals were grown by mixing equal volumes of well solution (100 mM HEPES pH 7.5, 23% PEG 3350, 5 mM TCEP) and protein (60 mg/mL in 20 mM HEPES pH 7.5, 100 mM NaCl, 0.5 mM TCEP) in the hanging-drop format. |