5HSF

1.52 Angstrom Crystal Structure of Fc fragment of Human IgG1.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2010-08-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.07809
Spacegroup name	P 1 21 1
Unit cell lengths	47.713, 43.880, 49.579
Unit cell angles	90.00, 92.64, 90.00

Refinement procedure

Resolution	27.440 - 1.520
R-factor	0.15875
Rwork	0.157
R-free	0.18832
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB-1HZH
RMSD bond length	0.010
RMSD bond angle	1.535
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.550
High resolution limit [Å]	1.520	1.520
Rmerge	0.055	0.626
Number of reflections	31266
<I/σ(I)>	19.3	2.3
Completeness [%]	99.4	98.5
Redundancy	3.3	2.9
CC(1/2)	0.719

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.3	295	Protein: 11.0 mg/ml, 0.25M Sodium chloride, 0.1M Tris HCl (pH 8.3); Screen: PEGs II (F4), 0.2M Ammonium sulfate, 0.1M Sodium acetate, 22% (w/v) PEG 4000