2E3X
Crystal structure of Russell's viper venom metalloproteinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2006-03-26 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.350, 91.730, 152.930 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.069 | 0.212 |
Number of reflections | 20716 | |
<I/σ(I)> | 17 | 7 |
Completeness [%] | 96.4 | 79.5 |
Redundancy | 6.3 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Droplets were prepared by mixing 1l of protein solution and 1l of reservoir solution (0.1M calcium acetate, 0.1M sodium cacodylate, 10% PEG8000, pH 6.5) supplemented with one fifth volume of 10% PEG3350 as an additive and were equilibrated, typically, for one week against 1ml of reservoir solution., VAPOR DIFFUSION, SITTING DROP, temperature 293K |