5VH3
Crystal structure of Fab fragment of the anti-TNFa antibody infliximab in a C-centered orthorhombic crystal form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-11-19 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 86.580, 138.820, 195.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.1617 |
Rwork | 0.160 |
R-free | 0.19960 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4g3y |
RMSD bond length | 0.006 |
RMSD bond angle | 0.788 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (dev_2229) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.050 |
High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
Rmerge | 0.126 | 0.066 | 0.539 |
Rmeas | 0.137 | 0.073 | 0.588 |
Number of reflections | 79590 | 971 | 5830 |
<I/σ(I)> | 10.52 | 19.81 | 3.7 |
Completeness [%] | 100.0 | 97.9 | 100 |
Redundancy | 6.246 | 5.554 | 6.289 |
CC(1/2) | 0.994 | 0.992 | 0.889 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | Fab at 10 mg/mL against Wiz 34 screen condition B4 20% PEG 3350, 0.2 M potassium citrate tribasic supplemented with 20% ethylene glycol as cryo-protectant, crystal tracking ID 267664b4, unique puck ID sdw5-2 |