5VL0

horse liver alcohol dehydrogenase complexed with NADH and N-benzyformamide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2006-10-19
Detector	ADSC QUANTUM 210
Wavelength(s)	1.000
Spacegroup name	P 1 21 1
Unit cell lengths	50.160, 180.290, 86.920
Unit cell angles	90.00, 106.18, 90.00

Refinement procedure

Resolution	19.950 - 1.200
R-factor	0.1586
Rwork	0.158
R-free	0.19850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1p1r
RMSD bond length	0.019
RMSD bond angle	2.061
Data reduction software	d*TREK
Data scaling software	d*TREK (9.9.9.8L)
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	19.950	19.950	1.240
High resolution limit [Å]	1.200	2.580	1.200
Rmerge	0.088	0.066	0.513
Rmeas	0.094	0.070	0.576
Total number of observations	2278017
Number of reflections	365139		23988
<I/σ(I)>	8.3	20.8	1.7
Completeness [%]	79.4	98.9	59.5
Redundancy	6.19	8.6	4.34

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	7	278	10 mg/ml enzyme dialyzed against 50 mM ammonium N-[tris(hydroxylmethyl)methyl]2-aminoethane sulfonate (pH 6.7 at 25 deg C) with 1 mM NADH and 10 mM N-benzylformamide as the concentration of 2-methyl-2,4-pentanediol was raised to 25 %. Crystas was mounted on a fiber loop and flash vitrified by plunging it into liquid N2.