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1II0

CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-02-21
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameP 21 21 2
Unit cell lengths76.727, 222.189, 74.126
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution28.610 - 2.400
R-factor0.21
Rwork0.210
R-free0.25200
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.006
RMSD bond angle1.600
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 Overall
Low resolution limit [Å]28.600
High resolution limit [Å]2.400
Rmerge0.076
Total number of observations316955

*

Number of reflections46952

*

<I/σ(I)>16.9
Completeness [%]90.0
Redundancy6.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP830

*

PEG3000, ATP, MgCl2, NaAsO2, CdCl2, Bistrispropane, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 303K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21dropADP2 (mM)
31drop1 (mM)
41drop2 (mM)
51drop1 (mM)
61dropBis-Tris propane10 (mM)
71reservoirPEG30004 (%(w/v))
81reservoirBis-Tris propane100 (mM)

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PDB entries from 2024-05-15

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