3TDA

Competitive replacement of thioridazine by prinomastat in crystals of cytochrome P450 2D6

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-04-17
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	57.050, 192.740, 247.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.040 - 2.670
R-factor	0.217
Rwork	0.217
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3qm4
RMSD bond length	0.009
RMSD bond angle	1.300
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	CNS (1.3)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.186	2.810
High resolution limit [Å]	2.668	2.670
Rmerge	0.063	0.246
Number of reflections	79005
<I/σ(I)>	6.3	2.8
Completeness [%]	99.9	99.9
Redundancy	3.9	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	PEG3350, sodium acetate, sodium cacodylate, potassium phosphate, sodium chloride, zinc chloride, glycerol, beta-mercaptoethanol, prinomastat, thioridazine, HEGA-10, facial amphiphile 231_CHOL, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, prinomastat was added after protein crystallization