1QLH

HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-05-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	55.070, 73.720, 180.490
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.070
R-factor	0.209
Rwork	0.209
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hld
RMSD bond length	0.007
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	2.180
High resolution limit [Å]	2.070	2.070
Rmerge	0.112 *	0.301 *
Total number of observations	44823 *
Number of reflections	18016
<I/σ(I)>	4.8	2.4
Completeness [%]	79.2	57.4
Redundancy	2.5	2.4

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

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	10 (mg/ml)
2	1	2	MPD	12 (%)
3	1	2	ammonium N-[tris(hydroxymethyl)methyl]-2-aminoethanesulfonate buffer	50 (mM)
4	1	2	NAD+	1.3 (mM)
5	1	2	2,2,2-trifluoroethanol	400 (mM)