1F23
CONTRIBUTION OF A BURIED HYDROGEN BOND TO HIV-1 ENVELOPE GLYCOPROTEIN STRUCTURE AND FUNCTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 1999-09-24 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 1 |
Unit cell lengths | 38.920, 41.870, 55.980 |
Unit cell angles | 90.59, 88.93, 96.28 |
Refinement procedure
Resolution | 50.000 - 2.300 |
R-factor | 0.191 * |
Rwork | 0.191 |
R-free | 0.27000 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.076 | 0.287 |
Total number of observations | 62249 * | |
Number of reflections | 14667 | |
<I/σ(I)> | 7.7 | |
Completeness [%] | 96.1 | 92.8 |
Redundancy | 2 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | Sodium citrate, PEG 4000, propanol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | sodium citrate | 0.1 (M) | |
3 | 1 | reservoir | propanol | 5 (%) | |
4 | 1 | reservoir | PEG4000 | 7 (%) |