3MOQ
Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks
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 | 2009-04-28 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.95664 |
| Spacegroup name | P 32 |
| Unit cell lengths | 79.653, 79.653, 85.457 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 26.070 - 2.054 |
| R-factor | 0.19291 |
| Rwork | 0.190 |
| R-free | 0.24892 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ver |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.306 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.329 | 2.090 |
| High resolution limit [Å] | 2.054 | 2.050 |
| Rmerge | 0.068 | 0.928 |
| Number of reflections | 35851 | |
| <I/σ(I)> | 24.09 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.7 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 20% PEG 6000, 0.2M AMMONIUM CHLORIDE, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
