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4AZ0

crystal structure of cathepsin a, complexed with 8a.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID29
Synchrotron siteESRF
BeamlineID29
Temperature [K]100
Detector technologyCCD
Collection date2007-12-06
DetectorADSC CCD
Spacegroup nameC 1 2 1
Unit cell lengths90.530, 101.638, 48.179
Unit cell angles90.00, 101.97, 90.00
Refinement procedure
Resolution44.280 - 2.170
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)MODEL DERIVED FROM PDB ENTRY 1IVY
RMSD bond length0.007
RMSD bond angle0.950
Data reduction softwareXDS
Data scaling softwareXSCALE
Refinement softwareBUSTER (2.11.2)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]66.4602.260
High resolution limit [Å]2.1602.160
Rmerge0.0600.320
Number of reflections22196
<I/σ(I)>14.63.5
Completeness [%]96.979.2
Redundancy3.72.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.6277CATA WAS CRYSTALLIZED USING THE HANGING DROP METHOD: 1 UL OF PROTEIN SOLUTION, CONTAINING 6.5 MG/ML CATHEPSIN A, 25 MM TRIS-HCL (PH 8.0) AND 300 MM NACL, WAS MIXED WITH 1 UL RESERVOIR SOLUTION, CONTAINING 100 MM NAACETATE (PH 4.5), 18-20% PEG400 AND 100 MM CDCL2, AND SET TO EQUILIBRATE AT 4 DEG. C. ROD-SHAPED CRYSTALS APPEARED IN ABOUT ONE WEEK.

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