1P52
Structure of Arginine kinase E314D mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS II |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.393, 70.312, 80.139 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.900 |
| R-factor | 0.18 |
| Rwork | 0.178 |
| R-free | 0.23520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bg0 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.020 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.066 * | |
| Number of reflections | 27680 | |
| Completeness [%] | 98.0 * | 91.6 |
| Redundancy | 7.8 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 | 4 * | peg 6000, hEPES, MgCl2, ADP, NO3, ARGININE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | PEG6000 | 32 (%) | |
| 3 | 1 | drop | HEPES | 0.025 (M) | pH7.5 |
| 4 | 1 | drop | 0.05 (M) | ||
| 5 | 1 | drop | PEG6000 | 16 (%) | |
| 6 | 1 | reservoir | PEG6000 | 28 (%) |
