3FTN

Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-17
Detector	ADSC QUANTUM 4
Wavelength(s)	0.933
Spacegroup name	P 1 21 1
Unit cell lengths	79.376, 83.003, 119.691
Unit cell angles	90.00, 99.93, 90.00

Refinement procedure

Resolution	39.180 - 2.192
R-factor	0.1663
Rwork	0.165
R-free	0.22820
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.090
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.240
High resolution limit [Å]	2.200	5.970	2.200
Rmerge	0.092	0.058	0.349
Number of reflections	76750
<I/σ(I)>	11.597
Completeness [%]	97.8	95.4	99.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	8 mg/mL protein, 25 mM Tris-HCl, 50 mM NaCl, 0.1 mM DTT, 50 mM ZnCl2 (pH=7.5)] was mixed with 1 microliter of reservoir solution [16% (w/v) PEG8K, 200 mM magnesium acetate tetrahydrate, 100 mM Cacodylate buffer (pH 6.5), vapor diffusion, hanging drop, temperature 298K