1H3W

Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-09-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	49.550, 149.250, 75.750
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.820 *
R-factor	0.279
Rwork	0.279
R-free	0.32000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fc1
RMSD bond length	0.008
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.820
Rmerge	0.082	0.538 *
Number of reflections	6718
Completeness [%]	97.5	75.6 *
Redundancy	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6 *	4 *	DIALYSIS AGAINST WATER, pH 6.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	MES/Tris	20 (mM)	pH6
3	1	reservoir	sodium acetic acid	0.1 (M)	pH4.5
4	1	reservoir		2 (M)