6GB1

Crystal structure of the GLP1 receptor ECD with Peptide 11

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-04-09
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.999920
Spacegroup name	P 43 21 2
Unit cell lengths	55.550, 55.550, 138.830
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.570 - 2.730
R-factor	0.208
Rwork	0.205
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3c59
RMSD bond length	0.010
RMSD bond angle	1.180
Data reduction software	XDS ((VERSION November 3)
Data scaling software	autoPROC ((Version 1.1.6))
Phasing software	PHASER
Refinement software	BUSTER (2.11.7)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	51.570	2.870
High resolution limit [Å]	2.730	2.730
Rmerge	0.075	1.096
Number of reflections	6336
<I/σ(I)>	22	2.3
Completeness [%]	100.0	100
Redundancy	12	12.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	292	A 6-fold excess of peptide 11 was dissolved in a solution of 12 mg/ml GLP1R-ECD in 10 mM Tris buffer pH 7.5, 100 mM NaSulfate and 2% glycerol. 100 nl of this protein solution plus 100 nl reservoir solution were equilibrated against reservoir solution consisting of 10 mM CoCl2, 9.4 % (v/v) 1,6-hexanediol and 100 mM NaAcetate, pH 4.8. Crystals appeared after about one week.