1DQD

CRYSTAL STRUCTURE OF FAB HGR-2 F6, A COMPETITIVE ANTAGONIST OF THE GLUCAGON RECEPTOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-07-01
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	76.140, 133.740, 37.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.217 *
Rwork	0.217
R-free	0.31500
RMSD bond length	0.011 *
RMSD bond angle	2.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.053	0.319 *
Total number of observations	173940 *
Number of reflections	22946
<I/σ(I)>	10.4
Completeness [%]	98.1	95.4
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8 *	291	24% (w/w) PEG 2KME, 100mM Tris HCl , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)
3	1	reservoir	PEG MME2000	24 (%(w/w))
4	1	reservoir	Tris-HCl	100 (mM)