1QMG

Acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxy-methylvalerate, manganese and ADP-ribose.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-06-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	110.800, 61.200, 161.700
Unit cell angles	90.00, 95.00, 90.00

Refinement procedure

Resolution	10.000 - 1.600
R-factor	0.193 *
Rwork	0.196
R-free	0.22500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1yve
RMSD bond length	0.008
RMSD bond angle	1.700 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.000	1.640
High resolution limit [Å]	1.600	1.600
Rmerge	0.054 *	0.096 *
Number of reflections	299230
<I/σ(I)>	18.8	14.6
Completeness [%]	96.6	96.6
Redundancy	2.9	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	20 *	Dumas, R., (1994) J. Mol. Biol., 242, 578. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein		0.020mg
2	1	drop	HEPES-KOH	20 (mM)
3	1	reservoir	ammonium sulfate	2 (M)
4	1	reservoir	Tris-HCl	0.1 (M)