2C9Y
Structure of human adenylate kinase 2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-18 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.042, 49.260, 127.001 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.100 |
| R-factor | 0.198 |
| Rwork | 0.194 |
| R-free | 0.27400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ak2 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.768 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.140 | 0.580 |
| Number of reflections | 17233 | |
| <I/σ(I)> | 10.8 | 3 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7.12 | 6.98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.7 | 0.1 M BIS-TRIS PH=5.7, 28% PEG3350, pH 5.70 |
