6UHA
Open-form Crystal Structure of Human RYR Receptor 3 ( 848-1055)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-03-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97927 |
Spacegroup name | I 41 |
Unit cell lengths | 94.495, 94.495, 116.895 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.248 - 2.855 |
R-factor | 0.2248 |
Rwork | 0.223 |
R-free | 0.26780 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4rev |
RMSD bond length | 0.005 |
RMSD bond angle | 0.901 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | HKL-3000 |
Refinement software | PHENIX (1.11.1-2575_1309) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.900 |
High resolution limit [Å] | 2.850 | 7.730 | 2.850 |
Rmerge | 0.062 | 0.044 | 0.668 |
Rmeas | 0.075 | 0.053 | 0.834 |
Rpim | 0.042 | 0.029 | 0.491 |
Total number of observations | 31797 | ||
Number of reflections | 11458 | 548 | 570 |
<I/σ(I)> | 7.2 | ||
Completeness [%] | 96.0 | 87.8 | 98.8 |
Redundancy | 2.8 | 3 | 2.6 |
CC(1/2) | 0.970 | 0.498 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 297 | PEG3350 15%, protein in co-crystallization with 30mM Caffeine and 10mM ATP |