1H9M

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	1999-06-15
Detector	MARRESEARCH
Spacegroup name	H 3
Unit cell lengths	81.960, 81.960, 93.417
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 - 1.650
R-factor	0.191 *
Rwork	0.191
R-free	0.22600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h9j
RMSD bond length	0.026
RMSD bond angle	0.038
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.000	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.044	0.107
Number of reflections	28231
<I/σ(I)>	41.7	8.8
Completeness [%]	100.0	100
Redundancy	12.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5		VAPOUR DIFFUSION. 20% PEG 4000, 5% ISOPROPANOL IN 100MM HEPES PH7.5 WITH 2MM NA2MOO4., pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	20 (%(w/v))
2	1	reservoir	isopropanol	5 (%(v/v))
3	1	reservoir	HEPES	100 (mM)	pH7.5
4	1	reservoir		2 (mM)