3AAZ
Crystal structure of the humanized recombinant Fab fragment of a murine; antibody
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-25 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9566 |
| Spacegroup name | P 31 |
| Unit cell lengths | 106.732, 106.732, 90.867 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.030 - 2.200 |
| R-factor | 0.21247 |
| Rwork | 0.209 |
| R-free | 0.27134 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bae 1um5 8fab |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.742 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.030 | 2.260 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.090 | 0.430 |
| Number of reflections | 51677 | |
| <I/σ(I)> | 16.5 | 2 |
| Completeness [%] | 92.5 | 64.1 |
| Redundancy | 3.7 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 298 | 20% PEG 3350, 0.2M sodium sulfate, 0.2M lithium citrate, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
