5WAT
Corynebacterium glutamicum Full length Homoserine kinase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-02-09 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 68.081, 130.078, 195.951 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.335 - 2.141 |
| R-factor | 0.1909 |
| Rwork | 0.189 |
| R-free | 0.22470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4rpf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.134 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 42.340 |
| High resolution limit [Å] | 2.141 | 2.141 |
| Rmerge | 0.068 | 0.279 |
| Number of reflections | 48115 | 4566 |
| <I/σ(I)> | 20.6 | 4.1 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 4.7 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | protein in 20 mM Tris pH 7.5, 150 mM NaCl, 50 mM KCl and 50 mM MgCl2 well solution: 0.25 M ammonium sulfate, 25 % PEG 3,350 and 0.1 M HEPES pH 7.5 |
