2H9G
Crystal structure of phage derived Fab BdF1 with human Death Receptor 5 (DR5)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-03-14 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 99.814, 61.389, 108.269 |
Unit cell angles | 90.00, 101.17, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.320 |
R-factor | 0.2338 |
Rwork | 0.228 |
R-free | 0.28164 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Chain S from 1d0g Chain AB from 1FVE |
RMSD bond length | 0.010 |
RMSD bond angle | 1.300 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 54784 | |
<I/σ(I)> | 6.7 | 2 |
Completeness [%] | 97.1 | 97.3 |
Redundancy | 3.4 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 292 | Crystals from drops containing an equal volume of protein and well solution consisting of 20% PEG 3350, 0.2M Na2HPO4, 0.1 M Bis-Tris, pH 6.1-6.8. The crystals were cryo-protected with well solution supplemented with 20% PEG 200., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |