1I0E
CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 291 |
| Detector technology | DIFFRACTOMETER |
| Detector | WEISSENBERG |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 31 1 2 |
| Unit cell lengths | 89.326, 89.326, 402.962 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 3.500 |
| R-factor | 0.211 |
| Rwork | 0.211 |
| R-free | 0.28600 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | rabbit muscle creatine kinase |
| RMSD bond length | 0.008 |
| RMSD bond angle | 22.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.620 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.118 | 0.344 |
| Total number of observations | 63933 * | |
| Number of reflections | 21262 | |
| <I/σ(I)> | 2 | |
| Completeness [%] | 0.9 | 93.5 * |
| Redundancy | 3 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.8 * | 291 | Tang, L., (1998) Acta Crystallogr., D55, 669. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | pH5.8 |
| 2 | 1 | drop | MPD | 40 (%) | |
| 3 | 1 | reservoir | MPD | 40 (%) |
