1I92

STRUCTURAL BASIS OF THE NHERF PDZ1-CFTR INTERACTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	2000-11-20
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 31 2 1
Unit cell lengths	51.658, 51.658, 66.966
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	26.810 - 1.700
R-factor	0.187 *
Rwork	0.187
R-free	0.21700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1g9o
RMSD bond length	0.018
RMSD bond angle	1.800 *
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]	26.810	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.053	0.300
Total number of observations	110148 *
Number of reflections	10950
<I/σ(I)>	27.6	4
Completeness [%]	92.6	40 *
Redundancy	9.9	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	20 *	Sodium Acetate, Sodium Chloride, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	18 (mg/ml)
2	1	reservoir	sodium acetate	0.1 (M)
3	1	reservoir		2 (M)