7LF5

Structure of Hyperglycosylated Human IgG1 Fc (Fc267)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-09-06
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.033200
Spacegroup name	C 2 2 21
Unit cell lengths	51.379, 146.831, 75.917
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.390 - 2.600
R-factor	0.2247
Rwork	0.224
R-free	0.24270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4cdh
RMSD bond length	0.010
RMSD bond angle	1.331
Data reduction software	XDS (1.18.2_3874)
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.390	2.720
High resolution limit [Å]	2.600	2.600
Rmerge	0.021
Rpim	0.022	0.387
Number of reflections	9106	1110
<I/σ(I)>	13.9	2
Completeness [%]	99.4
Redundancy	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		298	CRYSTALS GROWN BY MIXING 1 UL OF FC267 (10 MG/ML IN 10mM HEPES, 75mM NaCl pH 7.4) WITH 1 UL OF PRECIPITANT SOLUTION CONSISTING OF 0.1M HEPES pH 6.5, 8% w/v PEG6000