1A72

AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD ANALOG CPAD

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	275
Detector technology	AREA DETECTOR
Collection date	1993-12-15
Detector	XENTRONICS
Spacegroup name	C 2 2 21
Unit cell lengths	55.500, 74.200, 179.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.600
R-factor	0.176
Rwork	0.176
R-free	0.30000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	8adh
RMSD bond length	0.013
RMSD bond angle	25.300 *
Data reduction software	XDS
Data scaling software	X-GEN
Phasing software	X-PLOR (3.0)
Refinement software	X-PLOR (3.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	22.000	2.680
High resolution limit [Å]	2.600	2.560
Rmerge	0.078
Total number of observations	16939 *
Number of reflections	10388
<I/σ(I)>	6	2
Completeness [%]	76.9	43

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8.4	4 *	CRYSTALS GROWN FROM 4 MICROLITER HANGING DROPS OF 10MG/ML PROTEIN IN 50 MM TRIS BUFFER (PH8.4 @4C) 4% (V/V) ETOH EQUILIBRATED AT 4C WITH WELLS CONTAINING 11-13% ETOH, vapor diffusion - hanging drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	13 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)
3	1	drop	PEG400	4 (%(v/v))
4	1	drop	NAD	5 (mM)
5	1	reservoir	Tris-HCl	50 (mM)
6	1	reservoir	PEG400	18 (%(v/v))