8TE5

Crystal structure of a multiple lysine-to-arginine substitution mutant of the human CRIg C3b-binding domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-11-01
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	31.006, 49.776, 60.029
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.015 - 1.502
R-factor	0.1713
Rwork	0.166
R-free	0.22340
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.799
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((1.14_3260: ???))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.550
High resolution limit [Å]	1.500	3.230	1.500
Rmerge	0.152	0.106	0.801
Rmeas	0.165	0.114	0.888
Rpim	0.061	0.041	0.376
Total number of observations	105683
Number of reflections	15185	1652	1484
<I/σ(I)>	10.1
Completeness [%]	99.1	98.9	99.5
Redundancy	7	7.5	5.4
CC(1/2)	0.996	0.987	0.702

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	0.1 M sodium aaetate (pH 6.5) 0.2 M ammonium acetate 30% (w/v) peg-4000