9MEG

Conformational flexibility in HLA-B8: peptide tuning structural and dynamical changes

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	100
Detector technology	CCD
Collection date	2024-01-31
Detector	MAR CCD 300 mm
Wavelength(s)	0.87313
Spacegroup name	P 21 21 21
Unit cell lengths	50.930, 81.440, 110.820
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.580 - 1.610
R-factor	0.20215
Rwork	0.201
R-free	0.22657
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6p2s
RMSD bond length	0.011
RMSD bond angle	1.876
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.270	1.650
High resolution limit [Å]	1.610	1.610
Rmerge	0.099	0.330
Number of reflections	56986	15283
<I/σ(I)>	10.7	3.3
Completeness [%]	99.5	99.5
Redundancy	7.5	6.5
CC(1/2)	0.995

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	50% PEG4000, 20% citrate acid pH5.5, 0.1M ammonium acetate