7N05
Crystal structure of the F240 antibody fragment bound to the HIV-1 gp41 immunodominant region
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-05 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 46.072, 168.748, 78.367 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.697 - 1.700 |
| R-factor | 0.1732 |
| Rwork | 0.172 |
| R-free | 0.20380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7n04 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.066 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.27) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.070 | 46.070 | 1.730 |
| High resolution limit [Å] | 1.700 | 9.000 | 1.700 |
| Rmerge | 0.126 | 0.031 | 2.943 |
| Rmeas | 0.131 | 0.032 | 3.106 |
| Rpim | 0.035 | 0.009 | 0.973 |
| Total number of observations | 916192 | 6675 | 26639 |
| Number of reflections | 66334 | 558 | 2701 |
| <I/σ(I)> | 16.1 | 55.5 | 0.8 |
| Completeness [%] | 97.4 | 99.6 | 77.7 |
| Redundancy | 13.8 | 12 | 9.9 |
| CC(1/2) | 0.999 | 1.000 | 0.219 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293 | 0.17 M ammonium acetate, 0.085 M sodium citrate-HCl, pH 5.6, 25.5% (w/v) PEG 4000, and 15% (v/v) glycerol |
