2BBA
Crystal Structure and Thermodynamic Characterization of the EphB4 Receptor in Complex with an ephrin-B2 Antagonist Peptide Reveals the Determinants for Receptor Specificity.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-05-25 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 60.972, 60.972, 151.681 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.650 |
R-factor | 0.1761 |
Rwork | 0.174 |
R-free | 0.19135 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nuk |
RMSD bond length | 0.018 |
RMSD bond angle | 1.731 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Number of reflections | 32786 | |
<I/σ(I)> | 42.7 | 7.2 |
Redundancy | 3.7 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 293 | 2.2 M Ammonium Sulfate, 200 mM NaCl, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |