8P6Q

Racemic structure of TNFR1 cysteine-rich domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-07-24
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.6767
Spacegroup name	P 1 21 1
Unit cell lengths	20.420, 50.490, 46.210
Unit cell angles	90.00, 92.94, 90.00

Refinement procedure

Resolution	34.060 - 1.400
R-factor	0.20274
Rwork	0.200
R-free	0.25144
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.662
Data reduction software	xia2
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0411)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.060	1.420
High resolution limit [Å]	1.400	1.400
Number of reflections	18553	898
<I/σ(I)>	11.3	1
Completeness [%]	100.0	100
Redundancy	6.01
CC(1/2)	0.999	0.785

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	292	250 nL of DL-TNFR-1 CRD2 (25 mg/mL) and 250 nL of precipitant (1.5 M Sodium chloride, 10% v/v ethanol, pH 8.5) were mixed in the sitting drop. The single, block shaped crystal was dipped into 2.0 M lithium sulfate and flash frozen in liquid nitrogen during harvesting.