2DG2
Crystal Structure of Mouse Apolipoprotein A-I Binding Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-06-15 |
Detector | SBC-3 |
Wavelength(s) | 0.97898 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 104.855, 125.745, 163.620 |
Unit cell angles | 90.00, 106.56, 90.00 |
Refinement procedure
Resolution | 80.000 - 2.450 |
R-factor | 0.20724 |
Rwork | 0.206 |
R-free | 0.22844 |
Structure solution method | SAD |
RMSD bond length | 0.021 |
RMSD bond angle | 1.729 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 80.000 | 2.540 |
High resolution limit [Å] | 2.450 | 2.500 |
Rmerge | 0.083 | 0.509 |
Number of reflections | 69794 | |
<I/σ(I)> | 22.4 | 2.4 |
Completeness [%] | 98.8 | 98.7 |
Redundancy | 4.4 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 1.5M ammonium sulfate, 0.1M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |