2DSG
Crystal structure of Lys26 to Arg mutant of Diphthine synthase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-18 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.00 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 105.142, 105.142, 137.151 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.21100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wng |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.069 | 0.283 |
Number of reflections | 52641 | |
<I/σ(I)> | 12.4 | 4.99 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.7 | 11.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.5 | 295 | 1.8M AMMONIUM SULFATE, 0.1M MES, 0.01M Co CHLORIDE, pH 6.5, microbatch, temperature 295K |