1QLJ

HORSE LIVER ALCOHOL DEHYDROGENASE APO ENZYME DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-04-15
Detector	RIGAKU IMAGE PLATE
Spacegroup name	P 21 21 21
Unit cell lengths	55.140, 72.920, 180.250
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.800
R-factor	0.226
Rwork	0.226
R-free	0.25700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hld
RMSD bond length	0.010
RMSD bond angle	20.100 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS (0.4)
Refinement software	CNS (0.4)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.130
High resolution limit [Å]	2.800	2.800
Rmerge	0.102 *	0.221 *
Total number of observations	49060 *
Number of reflections	17446
<I/σ(I)>	5.9	3.2
Completeness [%]	94.2	87.8
Redundancy	2.8	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	8.4 *	5 *	PROTEIN WAS CRYSTALLIZED BY THE BATCH DIALYSIS METHOD USING MPD AS THE PRECIPITANT AT PH 7.0, 50 MM AMMONIUM N-[TRIS(HYDROXYMETHYL)METHYL]-2 AMINOETHANESULFONATE, WITH 0.66 MM NADH AND 0.76 MM

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	10 (mg/ml)
2	1	2	MPD	4.5 (%)
3	1	2	tris(hydroxymethyl)aminomethane-HCl	50 (mM)