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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 methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
Collection date1999-06-15
DetectorMARRESEARCH
Spacegroup nameH 3
Unit cell lengths81.960, 81.960, 93.417
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution40.000 - 1.650
R-factor0.191

*

Rwork0.191
R-free0.22600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1h9j
RMSD bond length0.026
RMSD bond angle0.038
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]41.0001.680
High resolution limit [Å]1.6501.650
Rmerge0.0440.107
Number of reflections28231
<I/σ(I)>41.78.8
Completeness [%]100.0100
Redundancy12.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION7.5VAPOUR DIFFUSION. 20% PEG 4000, 5% ISOPROPANOL IN 100MM HEPES PH7.5 WITH 2MM NA2MOO4., pH 7.50
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG400020 (%(w/v))
21reservoirisopropanol5 (%(v/v))
31reservoirHEPES100 (mM)pH7.5
41reservoir2 (mM)

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PDB entries from 2024-05-15

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