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1K3B

Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyAREA DETECTOR
Collection date1998-06-30
DetectorMARRESEARCH
Wavelength(s)1.0
Spacegroup nameI 2 2 2
Unit cell lengths87.154, 88.031, 114.609
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 2.150
R-factor0.186
Rwork0.190
R-free0.23100
Structure solution methodMAD, MIR, MOL. REPL together
RMSD bond length0.009
RMSD bond angle1.540
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareMAIN
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.180
High resolution limit [Å]2.1502.150
Rmerge0.0700.249

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Total number of observations96833

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Number of reflections23553
Completeness [%]97.699

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Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP5.6293ammonium sulphate, sodium citrate, potassium/sodium tartrate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoirammonium sulfate2.0 (M)
31reservoirsodium citrate0.1 (M)
41reservoirpotassium/sodium tartrate0.2 (M)pH5.6

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PDB entries from 2024-09-18

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