7EQU

Crystal structure of the C-lobe of lactoferrin produced by limited proteolysis using pepsin at 2.74A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID30B
Synchrotron site	ESRF
Beamline	ID30B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-02-24
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9655
Spacegroup name	C 1 2 1
Unit cell lengths	153.759, 81.554, 111.364
Unit cell angles	90.00, 129.95, 90.00

Refinement procedure

Resolution	76.846 - 2.743
Rwork	0.239
R-free	0.29840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5hbc
RMSD bond length	0.007
RMSD bond angle	1.681
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	76.850	2.790
High resolution limit [Å]	2.740	2.740
Rmerge	0.060	0.030
Rmeas	0.070	0.040
Number of reflections	27187	1391
<I/σ(I)>	10.2
Completeness [%]	97.5
Redundancy	2.9
CC(1/2)	0.990	0.990

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	298	Magnesium acetate, 20% PEG 3350