6KY2
Crystal Structure of Arginine Kinase wild type from Daphnia magna
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
| Synchrotron site | PAL/PLS |
| Beamline | 7A (6B, 6C1) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-28 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.997, 57.893, 74.447 |
| Unit cell angles | 90.00, 100.09, 90.00 |
Refinement procedure
| Resolution | 46.230 - 1.870 |
| R-factor | 0.1894 |
| Rwork | 0.187 |
| R-free | 0.23010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bhl |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.363 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.230 | 1.970 |
| High resolution limit [Å] | 1.870 | 1.870 |
| Rmerge | 0.081 | 0.474 |
| Number of reflections | 26672 | 3872 |
| <I/σ(I)> | 10.3 | |
| Completeness [%] | 98.6 | 99.1 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 1.8M Phosphate |
