2VT4

TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	CCD
Collection date	2007-12-14
Detector	MARRESEARCH
Spacegroup name	P 1
Unit cell lengths	55.500, 86.800, 95.500
Unit cell angles	67.60, 73.30, 85.80

Refinement procedure

Resolution	45.100 - 2.700
R-factor	0.215
Rwork	0.212
R-free	0.26800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2rh1
RMSD bond length	0.013
RMSD bond angle	1.272
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	PHENIX ((PHENIX.PHASER))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.400	2.850
High resolution limit [Å]	2.700	2.700
Rmerge	0.140	0.670
Number of reflections	41499
<I/σ(I)>	5.8	1.5
Completeness [%]	96.2	95.7
Redundancy	1.8	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.1		VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.