5T4Z
STRUCTURE OF THE ANTI-HIV ANTIBODY DH501 THAT BINDS GP120 V3 GLYCAN AND THE BASE OF V3 WITH FREE MAN9 GLYCAN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2016-08-22 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.757, 115.997, 76.889 |
Unit cell angles | 90.00, 97.39, 90.00 |
Refinement procedure
Resolution | 34.485 - 1.991 |
R-factor | 0.189 |
Rwork | 0.187 |
R-free | 0.23870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5iie |
RMSD bond length | 0.009 |
RMSD bond angle | 1.186 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 34.490 |
High resolution limit [Å] | 1.990 |
Rmerge | 0.060 |
Number of reflections | 58802 |
<I/σ(I)> | 28.4 |
Completeness [%] | 100.0 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M CaCl2, 20% PEG 3350 |