9D7Y

Crystal structure of scFv corresponding to human autoantibody b96.11

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-08-15
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9537
Spacegroup name	P 21 21 21
Unit cell lengths	96.544, 103.963, 85.088
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.770 - 2.600
R-factor	0.2329
Rwork	0.227
R-free	0.30080
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.316
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX (1.20.1-4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.770	2.690
High resolution limit [Å]	2.600	2.600
Rmerge	0.137
Rpim		0.940
Number of reflections	26242	2526
<I/σ(I)>	3.92	0.68
Completeness [%]	85.7	70.06
Redundancy	1.9	1.9
CC(1/2)	0.968	0.362

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	The hanging drop contained 1 microliter of mother liquor combined with 1 microliter of 20 mg/mL b96.11 scFv protein solution. Crystals formed as shards within 24 hours at 293 K, with final crystals being selected from well conditions containing 0.1M Bis-Tris pH 6.5, 2.5M (NH4)2SO4