2QBX
EphB2/SNEW Antagonistic Peptide Complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-10-10 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | P 32 |
Unit cell lengths | 40.183, 40.183, 235.025 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.790 - 2.300 |
R-factor | 0.19793 |
Rwork | 0.194 |
R-free | 0.26950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nuk |
RMSD bond length | 0.017 |
RMSD bond angle | 2.106 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.790 | 2.300 |
High resolution limit [Å] | 2.299 | 2.299 |
Number of reflections | 17391 | |
Completeness [%] | 87.06 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 298 | 100 mM Hepes, pH 7.2, 100 mM ammonium sulfate, and 20% PEG-3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K |