1LDE

HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1995-04
Detector	RIGAKU
Spacegroup name	P 1 21 1
Unit cell lengths	49.930, 180.200, 86.800
Unit cell angles	90.00, 106.00, 90.00

Refinement procedure

Resolution	20.000 - 2.500
R-factor	0.205 *
Rwork	0.205
R-free	0.25600
RMSD bond length	0.030
RMSD bond angle	0.060
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.035 *	0.087 *
Number of reflections	94632
<I/σ(I)>	18.8	8.8
Completeness [%]	88.8	77.2
Redundancy	2.1	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	7	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 3-BUTYLTHIOLANE 1-OXIDE. VERY CLOSE TO C-CENTERED ORTHORHOMBIC BUT SCALES VERY BADLY AS C222. SO THE SYMMETRY IS ACTUALLY P21., batch dialysis

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	alcohol dehydrogenase	10 (mg/ml)
2	1	reservoir	ammonium N-[tris(hydroxymethyl)methyl]-2-aminoethanesulfonate	50 (mM)
3	1	reservoir	NADH	0.66 (mM)
4	1	reservoir	N-formylpiperidine	14 (mM)
5	1	reservoir	MPD	25 (%)