3VSN
The crystal structure of novel chondroition lyase ODV-E66, baculovirus envelope protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.300 |
Spacegroup name | P 62 |
Unit cell lengths | 118.172, 118.172, 100.099 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.740 - 2.000 |
R-factor | 0.16775 |
Rwork | 0.166 |
R-free | 0.19421 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.046 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXS |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.700 |
Rmerge | 0.133 |
Number of reflections | 86407 |
Completeness [%] | 99.5 |
Redundancy | 11.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 50mM Tri-HCl pH8.0, 100mM NaCl, 0.02M citric acid, 0.08M Bis-Tris propane pH8.8, 18% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |