5VH5

Crystal Structure of Fc fragment of anti-TNFa antibody infliximab

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2015-10-22
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	C 2 2 21
Unit cell lengths	50.160, 148.030, 75.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.264 - 1.750
R-factor	0.1923
Rwork	0.190
R-free	0.22820
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4cdh
RMSD bond length	0.007
RMSD bond angle	0.856
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]	33.264	33.264	1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.055	0.039	0.544
Rmeas	0.060	0.044	0.595
Number of reflections	28936	336	2117
<I/σ(I)>	17.54	31.78	3.32
Completeness [%]	99.8	88.9	100
Redundancy	5.985	4.494	6.145
CC(1/2)	0.999	0.997	0.866

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		289	JCSG+ E7 (266855e7): 10% propanol-2, 200mM zinc acetate, 100mM sodium cacodylate pH6.5: protein conc. 10mg/mL: cryo 20% ethylene glycol: puckID sxt1-8