4OFR
Crystal structure of AR-LBD bound with co-regulator peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 150 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.751, 66.230, 71.101 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.710 - 2.260 |
R-factor | 0.19307 |
Rwork | 0.190 |
R-free | 0.25093 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4oea |
RMSD bond length | 0.012 |
RMSD bond angle | 1.519 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 25.710 |
High resolution limit [Å] | 2.260 |
Rmerge | 0.070 |
Number of reflections | 11769 |
Completeness [%] | 84.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 1.6M magnesium sulphate, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |