6C99

Crystal structure of FcRn bound to UCB-303

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	2015-02-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	41.770, 76.080, 140.040
Unit cell angles	90.00, 93.56, 90.00

Refinement procedure

Resolution	46.590 - 2.000
R-factor	0.1905
Rwork	0.189
R-free	0.22020
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.906
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.071	0.517
Number of reflections	59144	4319
<I/σ(I)>	13.96	2.5
Completeness [%]	99.8	99.9
Redundancy	3.8	3.8
CC(1/2)	0.998	0.837

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3	289	APO FCRN CRYSTALS WERE PRODUCED BY SITTING DROP VAPOR DIFFUSION WITH AN EQUAL VOLUME COMBINATION OF THE PROTEIN COMPLEX, PROVIDED IN A PROTEIN SOLUTION CONTAINING 50MM HEPES PH 7.0 AND 75MM NACL, AND AN OPTIMIZATION SCREEN CONTAINING 0.1M CITRIC ACID/NAOH PH 3.01-3.09 AND 12-16% W/V PEG 6,000. CRYSTALS OF FCRN WERE SOAKED FOR THREE DAYS IN BUFFER CONTAINING 0.1M CITRIC ACID/NAOH PH 3.0, 20% W/V PEG6,000, AND 20% GLYCEROL AND 12.5MM UCB-303.