1H9K

Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity. Phosphate-grown form with tungstate and phosphate bound

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	1998-04-15
Detector	MARRESEARCH
Spacegroup name	P 3 2 1
Unit cell lengths	50.685, 50.685, 79.112
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 - 1.800
R-factor	0.186 *
Rwork	0.186
R-free	0.22700
Structure solution method	MAD
RMSD bond length	0.013
RMSD bond angle	0.034
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.088	0.224
Number of reflections	10860
<I/σ(I)>	5.5	2.7
Completeness [%]	98.9	95.6
Redundancy	9.5	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8.5		VAPOUR DIFFUSION. 75% SATURATED KH2PO4 IN 100MM TRIS-HCL PH8.5 WITH 2MM NA2WO4., pH 8.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		75 (%sat)
2	1	reservoir	Tris-HCl	100 (mM)	pH8.5
3	1	reservoir		2 (mM)