5DYL
Crystal structure of the cGMP-dependent protein kinase PKG from Plasmodium Vivax - Apo form
Replaces: 4MYIExperimental 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 | 2013-07-25 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97945 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 192.471, 117.773, 67.682 |
| Unit cell angles | 90.00, 94.66, 90.00 |
Refinement procedure
| Resolution | 44.000 - 2.400 |
| R-factor | 0.2138 |
| Rwork | 0.212 |
| R-free | 0.24630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.083 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.27) |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 44.780 | 44.780 | 2.470 |
| High resolution limit [Å] | 2.400 | 10.460 | 2.400 |
| Rmerge | 0.101 | 0.074 | 0.907 |
| Rpim | 0.064 | 0.048 | 0.574 |
| Total number of observations | 201478 | 2373 | 15539 |
| Number of reflections | 58714 | ||
| <I/σ(I)> | 7.7 | 17.7 | 1.5 |
| Completeness [%] | 99.9 | 97.9 | 99.9 |
| Redundancy | 3.4 | 3.3 | 3.4 |
| CC(1/2) | 0.991 | 0.982 | 0.654 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 10% PEG 5000 MME, 5% Tacsimate ph7.0, 0.1 M Hepes ph7, 15 mM spermidine, 25% glycerol |
