1AFV
HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH FAB25.3
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 1995-12 |
Detector | PRINCETON 2K |
Spacegroup name | P 21 2 21 |
Unit cell lengths | 119.900, 92.300, 149.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 3.700 |
R-factor | 0.217 |
Rwork | 0.217 |
R-free | 0.32400 |
Structure solution method | MOLECULAR REPLACEMENT, MULTIPLE ISOMORPHOUS REPLACEMENT, ANOMALOUS DISPERSION |
Starting model (for MR) | FAB |
RMSD bond length | 0.007 |
RMSD bond angle | 24.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.064 | 0.370 |
Number of reflections | 29703 | |
Completeness [%] | 87.1 | 50.4 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7 | 16% PEG 3350, 50 MM BISTRIS-HCL, PH 7.0, 0.1% BETA-OCTYLGLUCOSIDE, 1 MM NAN3 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 20 (mM) | ||
2 | 1 | reservoir | PEG3350 | 12-24 (%) | |
3 | 1 | reservoir | Bis tris Cl | 40 (mM) | |
4 | 1 | reservoir | 20 (mM) |