1UC8
Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45PX |
| Synchrotron site | SPring-8 |
| Beamline | BL45PX |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-06-04 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.02 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 124.652, 51.366, 103.594 |
| Unit cell angles | 90.00, 122.81, 90.00 |
Refinement procedure
| Resolution | 43.500 * - 2.000 |
| Rwork | 0.240 |
| R-free | 0.26900 * |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 23.200 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.053 | 0.475 |
| Number of reflections | 37382 | |
| <I/σ(I)> | 12.8 | 2.9 |
| Completeness [%] | 99.6 | 99.9 |
| Redundancy | 4.2 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | Vassylyeva, M.N., (2003) Acta Crystallogr., D59, 1651. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 5 (%) | |
| 3 | 1 | reservoir | sodium acetate | 17 (mM) | pH4.6 |
| 4 | 1 | reservoir | ammonium acetate | 0.35 (mM) |
