3F58
IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 12-RESIDUE CYCLIC PEPTIDE (INCLUDING RESIDUES 315-324 OF HIV-1 GP120 (MN ISOLATE); H315S MUTATION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | MACSCIENCE M18X |
| Temperature [K] | 295 |
| Detector technology | AREA DETECTOR |
| Collection date | 1992-05-01 |
| Detector | SIEMENS |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 95.470, 115.460, 49.580 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.000 - 2.800 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | FAB PORTION OF 1ACY |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.500 |
| Data reduction software | X-GEN |
| Data scaling software | X-GEN |
| Phasing software | MERLOT |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.800 | 2.980 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.072 * | 0.218 * |
| Total number of observations | 47266 * | |
| Number of reflections | 13951 | 2259 * |
| <I/σ(I)> | 13.2 | 1.5 |
| Completeness [%] | 98.9 | 97.7 |
| Redundancy | 3.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5 | 22.5 * | pH 5.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG4000 | 16 (%) | |
| 2 | 1 | reservoir | imidazole malate | 0.2 (M) | |
| 3 | 1 | drop | peptide | 2.4 times Fab molar | |
| 4 | 1 | drop | Fab | 15 (mg/ml) |
