3SYQ
Crystal structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) R201A mutant in complex with PIP2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-24 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.034 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 87.605, 208.491, 117.376 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.390 - 3.440 |
| R-factor | 0.3006 |
| Rwork | 0.299 |
| R-free | 0.32270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e4f |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.019 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 49.390 | 49.386 | 3.570 |
| High resolution limit [Å] | 3.432 | 7.430 | 3.450 |
| Rmerge | 0.063 | 0.043 | |
| Number of reflections | 14690 | ||
| <I/σ(I)> | 9.1 | ||
| Completeness [%] | 100.0 | 99.7 | 100 |
| Redundancy | 7.9 | 11.8 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.25 | 293.15 | 50 mM HEPES sodium, pH 7.25, 0.5 M sodium chloride, 25% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K |
