1O0S

Crystal Structure of Ascaris suum Malic Enzyme Complexed with NADH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	100
Detector technology	CCD
Collection date	2001-06-18
Detector	ADSC QUANTUM 4
Wavelength(s)	0.992
Spacegroup name	P 31 2 1
Unit cell lengths	130.947, 130.947, 149.128
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.000
R-factor	0.223
Rwork	0.221
R-free	0.27200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1llq
RMSD bond length	0.015
RMSD bond angle	22.156 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.090
High resolution limit [Å]	2.000	2.000
Rmerge	0.056 *	0.528
Total number of observations	693156 *
Number of reflections	104791 *
<I/σ(I)>	21.6	2.77
Completeness [%]	98.7 *	98.4
Redundancy	6.75	2.74

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.3 *	298	PEG 4000, sodium acetate, sodium tartronate, NADH, magnesium sulphate, mercaptoethanol, tris, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-SO4	100 (mM)	pH7.3
2	1	reservoir	sodium acetate	100 (mM)
3	1	reservoir	PEG4000	15 (%)
4	1	reservoir	NADH	5 (mM)
5	1	reservoir	tartronate	10 (mM)
6	1	reservoir		20 (mM)
7	1	reservoir	2-mercaptoethanol	10 (mM)
8	1	reservoir	sodium azide	0.02 (%)