2DV7
Crystal structure of Lys187 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) | 1.0 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 105.837, 105.837, 138.156 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.300 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.24100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wng |
RMSD bond length | 0.007 |
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 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.104 | 0.362 |
Number of reflections | 35614 | |
<I/σ(I)> | 11.8 | 4.23 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.6 | 12 |
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 |