2O8N
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 | 2005-10-19 |
Detector | SBC-3 |
Spacegroup name | H 3 2 |
Unit cell lengths | 124.312, 124.312, 120.677 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 80.320 - 2.000 |
R-factor | 0.171 |
Rwork | 0.169 |
R-free | 0.19600 |
Structure solution method | SAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.596 |
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] | 80.320 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.111 | 0.653 |
Number of reflections | 24177 | |
<I/σ(I)> | 56.4 | 8.9 |
Completeness [%] | 100 | |
Redundancy | 13.7 | 12.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 293 | 0.1 M sodium acetate, 1.5 M ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 4.60 |