1KEO

TWISTS AND TURNS OF THE CD-MPR: LIGAND-BOUND VERSUS LIGAND-FREE RECEPTOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1998-01-09
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	I 4
Unit cell lengths	108.772, 108.772, 72.670
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.200
R-factor	0.215 *
Rwork	0.215
R-free	0.24830
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.240
High resolution limit [Å]	2.200	2.200
Rmerge	0.087	0.490
Total number of observations	83198 *
Number of reflections	11338 *
Completeness [%]	94.9	70.5
Redundancy	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5	19 *	25% PEG 5000 monomethyl ether, 0.2M ammonium acetate, 0.1M cacodoylate, 150 mM Nacl, 50 mM imidazole (pH=6.5), 10 mM Manganese chloride, 5 mM beta-glycerophosphate, VAPOR DIFFUSION, SITTING DROP, temperature 292K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG5000 MME	25 (%(w/v))
3	1	reservoir	ammonium acetate	0.2 (M)
4	1	reservoir	cacodylate	0.1 (M)	pH6.5