3O26

The structure of salutaridine reductase from Papaver somniferum.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2009-06-30
Detector	SBC-3
Wavelength(s)	0.97970
Spacegroup name	P 64 2 2
Unit cell lengths	139.906, 139.906, 100.174
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	37.458 - 1.910
R-factor	0.1934
Rwork	0.193
R-free	0.20840
Structure solution method	SAD
RMSD bond length	0.007
RMSD bond angle	1.077
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	PHENIX (1.6.1_353)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.000	1.960
High resolution limit [Å]	1.910	1.910
Number of reflections	40176
<I/σ(I)>		4.7
Completeness [%]	94.3	68
Redundancy		4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.3	277	0.1 M MES pH 6.0-6.6, 1.9 M ammonium sulfate, 5%(v/v) PEG400, 0.1 M LiCl, 3%(v/v) glycerol. 2uL of 6 mg/ml SeMet SalR in addition of 4 mM NADPH was mixed with 2uL of the reservoir solution, VAPOR DIFFUSION, HANGING DROP, temperature 277K