6CTC

Crystal structure of human transferrin bound to Triferic FPC iron pyrophosphate

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	2013-07-03
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	74.370, 90.160, 110.430
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.376 - 2.600
R-factor	0.1838
Rwork	0.180
R-free	0.25320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4h0w
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	34.376	34.376	2.670
High resolution limit [Å]	2.600	11.630	2.600
Rmerge	0.045	0.019	0.484
Rmeas	0.049	0.020	0.522
Number of reflections	23450	293	1713
<I/σ(I)>	31.55	72.77	4.7
Completeness [%]	99.9	93.3	100
Redundancy	7.038	5.341	7.248
CC(1/2)	1.000	1.000	0.929

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	Apo human transferrin (ProSpec pro-325 purified by Q-sepharose) at 56 mg/mL (0.76 mM) against Morpheus screen condition D4 12.5% PEG 1000, 12.5% PEG3350, 12.5% MPD, 0.02 M each 1,6-hexanediol, 1-butanol, RS-1,2-propanediol, 2-propanol, 1,4-butanediol, 1,3-propanediol, 0.1 M MES/imidazole pH 6.5, crystal tracking ID 246352d4, unique puck ID suv0-5