1WN1
Crystal Structure of Dipeptiase from Pyrococcus Horikoshii OT3
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-06-13 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 0.97929, 0.97950, 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.966, 89.002, 147.159 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.990 - 2.250 |
R-factor | 0.211 |
Rwork | 0.211 |
R-free | 0.24800 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.330 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.306 | |
Number of reflections | 35622 | |
Completeness [%] | 99.4 | 98.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | PEG400, Cacodylate-NaOH AND 15microlitre MgAcet, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |