1C1Z
CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-05-25 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 159.500, 164.800, 114.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.870 |
R-factor | 0.238 |
Rwork | 0.238 |
R-free | 0.24400 |
Structure solution method | MIR-MAD COMBINATION |
RMSD bond length | 0.009 |
RMSD bond angle | 24.570 * |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SHARP |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.050 |
High resolution limit [Å] | 2.870 | 2.870 |
Rmerge | 0.086 | 0.430 |
Total number of observations | 103699 * | |
Number of reflections | 32406 | |
Completeness [%] | 93.2 | 60.1 |
Redundancy | 3.2 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.2 | 277 | Saxena, A., (1998) Acta Crystallogr., Sect.D, 54, 1450. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 1.6-2.0 (M) | |
3 | 1 | reservoir | sodium carbonate | 0.2 (%) |