9NIH

Crystal structure of HLA-DR4 presenting citrullinated Tenascin C peptide

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	2021-12-03
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.95373
Spacegroup name	H 3
Unit cell lengths	119.300, 119.300, 73.273
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	34.530 - 2.400
R-factor	0.186
Rwork	0.184
R-free	0.21860
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.691
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.530	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.092	0.352
Rmeas	0.102	0.391
Rpim	0.045	0.170
Number of reflections	15161	1628
<I/σ(I)>	16.4	7.2
Completeness [%]	99.6	99.3
Redundancy	10.2	10.4
CC(1/2)	0.998	0.970

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	0.2 M NaCl, 0.1 M Bis Tris pH 5.5, 29% PEG3350