2XA8
Crystal structure of the Fab domain of omalizumab at 2.41A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-01-24 |
Detector | BRUKER |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.600, 73.851, 141.126 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.930 - 2.420 |
R-factor | 0.223 |
Rwork | 0.221 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vl5 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.978 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE: 1.6.3_473)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.500 |
High resolution limit [Å] | 2.410 | 2.410 |
Rmerge | 0.100 | 0.820 |
Number of reflections | 25869 | |
<I/σ(I)> | 14.6 | 1.43 |
Completeness [%] | 98.6 | 94.1 |
Redundancy | 4.8 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 2.0 M AMMONIUM SULFATE, 0.1 M NA HEPES PH 7.5, 2% W/V PEG400. |