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 |