5XHF
Crystal structure of Trastuzumab Fab fragment bearing p-azido-L-phenylalanine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 05A |
| Synchrotron site | NSRRC |
| Beamline | TPS 05A |
| Temperature [K] | 99 |
| Detector technology | CCD |
| Collection date | 2017-03-13 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.841, 80.067, 85.792 |
| Unit cell angles | 113.67, 92.35, 102.78 |
Refinement procedure
| Resolution | 42.443 - 3.205 |
| R-factor | 0.227 |
| Rwork | 0.219 |
| R-free | 0.29660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n8z |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.482 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 3.200 |
| Number of reflections | 14758 |
| <I/σ(I)> | 2.45 |
| Completeness [%] | 95.7 |
| Redundancy | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | PEG 20000, MES-Na |
