3FSR

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	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2004-08-11
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	79.291, 101.427, 113.169
Unit cell angles	90.00, 94.19, 90.00

Refinement procedure

Resolution	39.418 - 2.200
R-factor	0.164
Rwork	0.161
R-free	0.22000
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	0.109	0.032	0.620
Number of reflections	90320
<I/σ(I)>	11.363
Completeness [%]	99.7	97.1	100
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	8mg/mL protein [25mM Tris-HCl, 50mM NaCl, 0.1mM DTT, 50mM ZnCl2 (pH=7.5)] was mixed with 0.001ml of reservoir solution [16% (w/v) PEG 8000, 200mM magnesium acetate tetrahydrate, 100mM Cacodylate buffer (pH 6.5)], vapor diffusion, hanging drop, temperature 298K