2XUU
Crystal structure of a DAP-kinase 1 mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-21 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.740, 84.430, 86.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 60.360 - 1.800 |
| R-factor | 0.1789 |
| Rwork | 0.176 |
| R-free | 0.22583 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w4k |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.009 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.410 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.110 | 0.560 |
| Number of reflections | 34469 | |
| <I/σ(I)> | 9.3 | 2.5 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 0.2 M LISO4 0.1 M BIS-TRIS PH 5.5 25% PEG 4000 0.002% NAN3 |
