3IOL

Crystal structure of Glucagon-Like Peptide-1 in complex with the extracellular domain of the Glucagon-Like Peptide-1 Receptor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-3
Synchrotron site	MAX II
Beamline	I911-3
Temperature [K]	100
Detector technology	CCD
Collection date	2008-11-26
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 21 2 21
Unit cell lengths	35.670, 42.670, 95.090
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.530 - 2.100
R-factor	0.18058
Rwork	0.178
R-free	0.22622
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3C59 without ligand
RMSD bond length	0.020
RMSD bond angle	1.681
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.5.0088)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	95.000	2.200
High resolution limit [Å]	2.100	2.100
Number of reflections	10348
<I/σ(I)>	14	5.3
Completeness [%]	98.0	98
Redundancy	7	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.9	291	0.1M N-(2-Acetamido) Iminodiacetic Acid (ADA), pH 6.9, 14 vol-% (+/-)-2-Methyl-2,4-pentanediol (MPD), 9mM n-decyl-beta-D-thiomaltoside, VAPOR DIFFUSION, HANGING DROP, temperature 291K