1HMS
1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.650, 55.450, 71.560 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.400 |
R-factor | 0.121 |
Rwork | 0.121 |
RMSD bond length | 0.019 |
RMSD bond angle | 2.660 |
Phasing software | X-PLOR |
Refinement software | SHELXL |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 31.200 * |
High resolution limit [Å] | 1.240 * |
Rmerge | 0.075 * |
Total number of observations | 78811 * |
Number of reflections | 32605 * |
Completeness [%] | 80.1 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.1 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25-30 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 28-30 (%) | |
3 | 1 | reservoir | piperazine-N-N'-bis[2-ethanesulfonic acid] | 20 (mM) |