5UTY
Crystal Structure of a Stabilized DS-SOSIP.mut4 BG505 gp140 HIV-1 Env Trimer, Containing Mutations I201C-P433C (DS), L154M, N300M, N302M, T320L in Complex with Human Antibodies PGT122 and 35O22 at 4.1 Angstrom
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-08-04 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1 |
| Spacegroup name | P 63 |
| Unit cell lengths | 131.447, 131.447, 312.348 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.481 - 3.412 |
| R-factor | 0.2437 |
| Rwork | 0.241 |
| R-free | 0.28820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4tvp |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.861 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.520 |
| High resolution limit [Å] | 3.400 | 7.320 | 3.400 |
| Rmerge | 0.149 | 0.070 | 1.136 |
| Rmeas | 0.158 | 0.074 | 1.305 |
| Rpim | 0.053 | 0.024 | 0.618 |
| Total number of observations | 199781 | ||
| Number of reflections | 25676 | ||
| <I/σ(I)> | 5.5 | ||
| Completeness [%] | 61.0 | 99.4 | 17.4 |
| Redundancy | 7.8 | 9.9 | 2.5 |
| CC(1/2) | 0.997 | 0.345 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 10.5% PEG 4000, 0.2M AmSO4, 0.1M NaoAc pH 4.6 |
