2CXF
RUN domain of Rap2 interacting protein x, crystallized in C2 space group
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 | CCD |
Collection date | 2004-10-03 |
Wavelength(s) | 0.97899, 0.97935, 0.96400 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 86.619, 41.592, 62.132 |
Unit cell angles | 90.00, 105.95, 90.00 |
Refinement procedure
Resolution | 14.990 - 3.070 |
R-factor | 0.237 |
Rwork | 0.237 |
R-free | 0.29100 |
Structure solution method | MAD |
RMSD bond length | 0.003 |
RMSD bond angle | 0.600 |
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 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Number of reflections | 3507 | |
<I/σ(I)> | 9.07169 | 6.35079 |
Completeness [%] | 88.4 | 63.2 |
Redundancy | 3.4069 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 300 | PEG20000, Bicine, Dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K |