1GG3

CRYSTAL STRUCTURE OF THE PROTEIN 4.1R MEMBRANE BINDING DOMAIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	110
Spacegroup name	C 1 2 1
Unit cell lengths	163.900, 106.500, 93.500
Unit cell angles	90.00, 95.50, 90.00

Refinement procedure

Resolution	20.000 - 2.800
R-factor	0.226
Rwork	0.226
R-free	0.27600
RMSD bond length	0.009
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.850
High resolution limit [Å]	2.800	2.800
Rmerge	0.048	0.360
Number of reflections	39441
<I/σ(I)>	16.9
Completeness [%]	99.8	98 *
Redundancy	6	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5.8	277	Han, B.G., (2000) Acta Crystallogr., D56, 187. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop		0.4 (M)
2	1	drop	PEG3000	3 (%)
3	1	reservoir		0.1 (M)