2HOW
Dipeptidase (PH0974) from Pyrococcus horikoshii OT3
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 | IMAGE PLATE |
Collection date | 2005-12-08 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.911, 88.820, 147.562 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.960 - 2.400 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.26500 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1wn1 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.112 | 0.365 |
Number of reflections | 29349 | |
Completeness [%] | 95.9 | 98.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | PEG400, CACODYLATE-NAOH, MAGNESIUM ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |