1DLB
HELICAL INTERACTIONS IN THE HIV-1 GP41 CORE REVEALS STRUCTURAL BASIS FOR THE INHIBITORY ACTIVITY OF GP41 PEPTIDES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1999-03-11 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | H 3 |
Unit cell lengths | 52.382, 52.382, 60.482 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.000 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.24300 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.800 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.040 |
Total number of observations | 23565 * |
Number of reflections | 4167 |
Completeness [%] | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 4.6 | 293 | PEG 4000, AMMONIUM SULPHATE, SODIUM ACETATE, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | peptide | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.6 |
4 | 1 | reservoir | PEG4000 | 11 (%) |