6UGY
Crystal structure of the Fc fragment of anti-TNFa antibody infliximab (Remicade) in a primative orthorhombic crystal form, Lot C
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 | 2015-11-05 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97857 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 50.340, 148.650, 75.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.181 |
Rwork | 0.178 |
R-free | 0.22830 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4cdh |
RMSD bond length | 0.008 |
RMSD bond angle | 0.920 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.086 | 0.034 | 0.558 |
Rmeas | 0.094 | 0.038 | 0.610 |
Number of reflections | 17056 | 222 | 1214 |
<I/σ(I)> | 15.26 | 37.24 | 3.28 |
Completeness [%] | 99.9 | 96.1 | 100 |
Redundancy | 6.101 | 4.662 | 6.18 |
CC(1/2) | 0.998 | 0.999 | 0.871 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | 10 mg/mL protein with JCSG+ E7 Opt screen H2 (267146h2): 4% 2-propanol, 200 mM zinc acetate, 100 mM sodium cacodylate, pH 6.8, cryoprotectant: 20% ethylene glycol, puckID kux1-9 |