3BDY
Dual specific bH1 Fab in complex with VEGF
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-07-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.00 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 100.600, 197.978, 77.650 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.600 |
R-factor | 0.197 |
Rwork | 0.194 |
R-free | 0.25200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1n8z |
RMSD bond length | 0.010 |
RMSD bond angle | 1.255 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 24705 | |
<I/σ(I)> | 16 | 3 |
Completeness [%] | 99.8 | 100 |
Redundancy | 6.2 | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 292 | For crystallization of the Fab/VEGF (8-109) complex, equal volumes of protein complex solution (10.6 mg/ml protein, 300 mM NaCl, 25 mM Tris-HCl pH 7.5) and crystallization buffer containing 0.15 D, L Malic Acid pH 7.0, 20% PEG3350 were mixed and equilibrated at 19 C. Prior to data collection the crystals were cryo-protected by transfer between drops containing 5%, 10% and 15% Glycerol in artificial mother liquor, followed by flash freeze in liquid nitrogen, VAPOR DIFFUSION, temperature 292K |