8W83

HLA-DQ2.5-alpha1 gliadin peptide in complex with DQN0344AE02

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-17A
Synchrotron site	Photon Factory
Beamline	BL-17A
Temperature [K]	95
Detector technology	PIXEL
Collection date	2018-03-14
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.980000
Spacegroup name	P 1 21 1
Unit cell lengths	87.488, 174.235, 129.656
Unit cell angles	90.00, 93.17, 90.00

Refinement procedure

Resolution	54.860 - 2.818
R-factor	0.28
Rwork	0.278
R-free	0.32090
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1s9v
RMSD bond length	0.004
RMSD bond angle	0.590
Data reduction software	XDS (Jan 31, 2020)
Data scaling software	Aimless (0.7.4)
Phasing software	PHASER
Refinement software	BUSTER (2.11.8 (8-JUN-2022))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	129.458	129.458	3.270
High resolution limit [Å]	2.818	9.881	2.818
Rmerge	0.500	0.090	1.237
Rmeas	0.547	0.099	1.358
Rpim	0.217	0.040	0.551
Total number of observations	285587	13372	13128
Number of reflections	44543	2227	2228
<I/σ(I)>	4.68	13.21	1.67
Completeness [%]	92.7	99.7	72.8
Completeness (spherical) [%]	47.7	99.7	6.7
Completeness (ellipsoidal) [%]	92.7	99.7	72.8
Redundancy	6.41	6	5.89
CC(1/2)	0.900	0.990	0.593
Anomalous completeness (spherical)	46.8	98.3	6.4
Anomalous completeness	91.6	98.3	71.8
Anomalous redundancy	3.3	3.2	3.0
CC(ano)	0.220	0.382	0.097
|DANO|/σ(DANO)	0.8	0.7	0.8

Diffraction limits	Principal axes of ellipsoid fitted to diffraction cut-off surface
4.256 Å	0.757, 0.757, 0.757
3.653 Å	0.000, 0.000, 0.000
2.817 Å	-0.653, -0.653, -0.653

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	294	0.1 M HEPES (pH7.5), 25.0 %w/v Polyethylene glycol 1,000, and 20 %v/v Glycerol as cryoprotectant