1XMI
Crystal structure of human F508A NBD1 domain with ATP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Detector technology | CCD |
Detector | MARRESEARCH |
Wavelength(s) | 0.9794 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 144.461, 154.022, 136.088 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.200 - 2.250 |
R-factor | 0.232 |
Rwork | 0.212 |
R-free | 0.26500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1r0x |
RMSD bond length | 0.006 |
RMSD bond angle | 0.997 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.524 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.128 | 0.017 |
Number of reflections | 71899 | |
<I/σ(I)> | 8.3 | 1.1 |
Completeness [%] | 99.8 | 99.4 |
Redundancy | 6.8 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 277 | PEG 400, glycerol, ethylene glycol, tris, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |