3M17

Crystal structure of human FcRn with a monomeric peptide inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Collection date	2007-09-01
Wavelength(s)	1.0
Spacegroup name	C 2 2 21
Unit cell lengths	114.320, 118.300, 248.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.100 - 2.600
R-factor	0.26408
Rwork	0.261
R-free	0.32548
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1exu
RMSD bond length	0.006
RMSD bond angle	0.962
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.100	2.690
High resolution limit [Å]	2.600	2.600
Number of reflections	51434
Completeness [%]	98.7	97.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1