4ZH9
Crystal Structure of the Domain-Swapped Dimer Wild-Type of Human Cellular Retinol Binding Protein II
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-15 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.978 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 36.851, 60.544, 64.021 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.989 - 2.660 |
R-factor | 0.2075 |
Rwork | 0.200 |
R-free | 0.27360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2rct |
RMSD bond length | 0.002 |
RMSD bond angle | 0.472 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.040 |
High resolution limit [Å] | 2.660 | 2.660 |
Rmerge | 0.059 | 0.731 |
Number of reflections | 4455 | |
<I/σ(I)> | 2.41 | |
Completeness [%] | 99.7 | 100 |
Redundancy | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | 25% PEG 4000 (40%), 0.1M Sodium Acetate pH 4.5, Ammonium Acetate 0.1M |