5VH4
Crystal structure of Fab fragment of anti-TNFa antibody infliximab in an I-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 | I 21 21 21 |
Unit cell lengths | 90.850, 93.610, 316.070 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.1594 |
Rwork | 0.158 |
R-free | 0.18650 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4g3y |
RMSD bond length | 0.006 |
RMSD bond angle | 0.864 |
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 | 0.081 | 0.026 | 0.654 |
Rmeas | 0.091 | 0.029 | 0.730 |
Number of reflections | 91050 | 1097 | 6634 |
<I/σ(I)> | 15.59 | 46.2 | 2.93 |
Completeness [%] | 99.8 | 95.1 | 99.9 |
Redundancy | 5.007 | 4.437 | 5.012 |
CC(1/2) | 0.998 | 0.999 | 0.803 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | Infliximab Fab at 10 mg/mL against 2.16 M sodium malonate, 10 mM NAD, crystal tracking ID 267666d9, unique puck ID sar8-4 |