1GQ4

STRUCTURAL DETERMINANTS OF THE NHERF INTERACTION WITH BETA2AR AND PDGFR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	115
Detector technology	IMAGE PLATE
Collection date	2001-06-29
Detector	RIGAKU RAXIS IV
Spacegroup name	P 31 2 1
Unit cell lengths	50.373, 50.373, 66.631
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	26.500 * - 1.900
R-factor	0.171 *
Rwork	0.171
R-free	0.18600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1i92
RMSD bond length	0.014
RMSD bond angle	1.650 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.500 *	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.059	0.194
Total number of observations	64231 *
Number of reflections	8069 *
<I/σ(I)>	23.4	8.4
Completeness [%]	99.8	99.7
Redundancy	5.4	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	4.24	20 *	CITRIC ACID, LITHIUM CHLORIDE, pH 4.24

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	19 (mg/ml)
2	1	reservoir	citric acid	0.1 (M)	pH4.24
3	1	reservoir		1 (M)