1F58
IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 1994-11-15 |
Detector | RIGAKU RAXIS II |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 72.890, 71.910, 88.250 |
Unit cell angles | 90.00, 98.31, 90.00 |
Refinement procedure
Resolution | 44.000 - 2.000 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | FAB 58.2 PORTION OF FAB 58.2/SER-LOOP PEPTIDE COMPLEX |
RMSD bond length | 0.010 |
RMSD bond angle | 1.800 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MERLOT |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.600 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.106 | 0.547 |
Total number of observations | 183103 * | |
Number of reflections | 30460 | 2014 * |
<I/σ(I)> | 29.5 | 3.4 |
Completeness [%] | 99.6 | 98.5 |
Redundancy | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.3 | 22.5 * | pH 6.3 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG10000 | 16 (%) | |
2 | 1 | reservoir | imidazole malate | 0.2 (M) | |
3 | 1 | drop | Fab | 15 (mg/ml) |