5UM4
Crystal structure of the F255A mutant Kir3.1 cytoplasmic pore domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-10-26 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0003 |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 80.070, 80.070, 85.040 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 85.040 - 2.500 |
R-factor | 0.2263 |
Rwork | 0.224 |
R-free | 0.26670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1n9p |
RMSD bond length | 0.010 |
RMSD bond angle | 1.137 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER (2.6.1) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 85.040 | 7.910 | 2.640 |
High resolution limit [Å] | 1.987 | 5.590 | 2.500 |
Rmerge | 0.040 | 0.591 | |
Rmeas | 0.067 | 0.042 | 0.615 |
Rpim | 0.019 | 0.012 | 0.169 |
Total number of observations | 125290 | ||
Number of reflections | 10030 | ||
<I/σ(I)> | 21.9 | 15.4 | 1.3 |
Completeness [%] | 99.6 | 100 | 100 |
Redundancy | 12.5 | 11.6 | 13.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | The protein was concentrated to 10 mg/mL. Crystals grown by mixing equal amounts of protein and reservoir solution (25 mM Na/K phosphate pH 5.0, 40 mM NaCl, 35 % Peg 400), and allowed to equilibrate over 1 ml of reservoir solution. |