1JP5
Crystal structure of the single-chain Fv fragment 1696 in complex with the epitope peptide corresponding to N-terminus of HIV-1 protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-05-12 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9340 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.490, 57.060, 91.040 |
| Unit cell angles | 90.00, 97.07, 90.00 |
Refinement procedure
| Resolution | 19.460 - 2.700 |
| R-factor | 0.229 |
| Rwork | 0.229 |
| R-free | 0.28700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | variable domains of Fab 1696 (PDB code 1CL7) |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.097 | 0.323 |
| Number of reflections | 12620 | |
| <I/σ(I)> | 6.06 | |
| Completeness [%] | 96.7 | 92.8 |
| Redundancy | 9.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 18 * | 0.05M tri-sodium citrate, 0.1M sodium phosphate, 24% PEG 3400, 0.2M ammonium sulphate, pH 5.5, VAPOR DIFFUSION, HANGING DROP at 292K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | tri-sodium citrate | 0.05 (M) | |
| 2 | 1 | reservoir | sodium phosphate | 0.1 (M) | pH5.5 |
| 3 | 1 | reservoir | PEG3400 | 24 (%) | |
| 4 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 5 | 1 | drop | peptide | 14 (mg/ml) |
