3APU
Crystal structure of the A variant of human alpha1-acid glycoprotein
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 | 2008-06-20 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 67.107, 44.862, 120.784 |
| Unit cell angles | 90.00, 91.88, 90.00 |
Refinement procedure
| Resolution | 31.990 - 2.100 |
| R-factor | 0.2012 |
| Rwork | 0.200 |
| R-free | 0.23168 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3BX6 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.336 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.044 | 0.326 |
| Number of reflections | 21258 | |
| <I/σ(I)> | 56.8 | 6.7 |
| Completeness [%] | 99.9 | 99.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 30% PEG 4000, 0.2M ammonium acetate, 0.1M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
