1AV1
CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I
Experimental procedure
Source type | ROTATING ANODE |
Source details | MACSCIENCE |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1996-01-24 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 97.470, 113.870, 196.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.000 - 4.000 |
R-factor | 0.382 |
Rwork | 0.382 |
R-free | 0.42800 |
Structure solution method | MIRAS |
RMSD bond length | 0.010 |
RMSD bond angle | 18.900 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | HASSP |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 4.220 |
High resolution limit [Å] | 4.000 | 4.000 |
Rmerge | 0.166 | 0.732 |
Number of reflections | 16089 | |
<I/σ(I)> | 3.7 | 0.9 |
Completeness [%] | 85.0 | 50 |
Redundancy | 3.6 | 1.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 1.2 M NA CITRATE, 100 MM HEPES, PH 7.5 AT 4 DEGREES CELSIUS. CRYSTALS WERE STABILIZED IN 1.4 M NA CITRATE, 100 MM HEPES, PH 7.5., temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | sodium citrate | 1.2 (M) |