2EBE
Crystal structure of Lys11 to Met mutant of hypothetical protein from Thermus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 180 |
| Detector technology | CCD |
| Collection date | 2006-10-07 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.460, 69.710, 73.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.680 - 1.800 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.25000 |
| Structure solution method | SAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.065 | 0.281 |
| Number of reflections | 22011 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6.9 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1M Bis-Tris, 25% PEG 2000 MME, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
