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1JNV

The Conformation of the Epsilon and Gamma Subunits within the E. coli F1 ATPase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL9-1
Synchrotron siteSSRL
BeamlineBL9-1
Temperature [K]100
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Wavelength(s)0.98
Spacegroup nameC 2 2 21
Unit cell lengths180.683, 197.517, 237.896
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution25.000 - 4.400
Rwork0.416
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1bmf 1fs0
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareAMoRE
Refinement softwareTNT
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0004.440
High resolution limit [Å]4.4004.400
Rmerge0.1220.358
Number of reflections17529
<I/σ(I)>3.72.1
Completeness [%]64.053.6
Redundancy5.15.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.225

*

Hausrath, A.C., (1999) Proc.Natl.Acad.Sci.U.S.J., 96, 13697.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
101dropATP0.1 (M)
111dropPEG80008.0 (%)
121reservoirammonium sulfate35 (%sat)
21dropTris-HCl110 (mM)
31dropglycerol10 (%)
41drop100 (mM)
51drop10 (mM)
61drop40 (mM)
71drop0.05 (%)
81dropEDTA0.1 (M)
91dropadenylylimidodiphosphate5 (mM)

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PDB entries from 2024-05-15

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