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1TYF

THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

Experimental procedure
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X12C
Synchrotron siteNSLS
BeamlineX12C
Temperature [K]110
Detector technologyCCD
Collection date1995-12
Spacegroup nameC 1 2 1
Unit cell lengths193.320, 102.460, 157.080
Unit cell angles90.00, 97.80, 90.00
Refinement procedure
Resolution80.000 - 2.300
R-factor0.219
Rwork0.219
R-free0.29200
RMSD bond length0.008
RMSD bond angle1.530
Data reduction softwareHKL ((DENZO))
Data scaling softwareHKL ((SCALEPACK))
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
Low resolution limit [Å]80.000

*

High resolution limit [Å]2.200

*

Rmerge0.077
Number of reflections142952

*

Completeness [%]100.0
Redundancy5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.5

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10.4 (mg/ml)
21dropHEPES10 (mM)
31drop200 (mM)
41dropdithiothreitol1 (mM)
51reservoirNa citrate100 (mM)
61reservoirPEG400010 (%(w/v))
71reservoirisopropanol20 (%(v/v))

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