1AGF
ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKRYKL-5R MUTATION)
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID2 |
| Synchrotron site | ESRF |
| Beamline | ID2 |
| Temperature [K] | 187 |
| Detector technology | CCD |
| Collection date | 1995-07-25 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.600, 81.300, 110.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.000 - 2.200 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HLA B27 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.076 * | 0.170 |
| Total number of observations | 140466 * | |
| Number of reflections | 26227 | |
| <I/σ(I)> | 5.7 | |
| Completeness [%] | 96.3 | 95.2 |
| Redundancy | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 21 * | Reid, S.W., (1996) Febs Lett., 383, 119. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris | 20 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 30 (%) | |
| 4 | 1 | reservoir | sodium citrate | 0.1 (M) | |
| 5 | 1 | reservoir | ammonium acetate | 0.03 (M) |
