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1I3P

THE 3.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A MUTATED BACULOVIRUS P35 AFTER CASPASE CLEAVAGE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL9-1
Synchrotron siteSSRL
BeamlineBL9-1
Temperature [K]170
Detector technologyIMAGE PLATE
Collection date1999-12-06
DetectorMARRESEARCH
Wavelength(s)0.98
Spacegroup nameP 32 2 1
Unit cell lengths75.806, 75.806, 120.693
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution14.950 - 3.100
R-factor0.239
Rwork0.239
R-free0.29100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1p35
RMSD bond length0.019
RMSD bond angle2.100
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0003.210
High resolution limit [Å]3.1003.100
Rmerge0.0540.395
Total number of observations80534

*

Number of reflections7577
<I/σ(I)>470.1
Completeness [%]99.099.6
Redundancy10.634.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7

*

25

*

9-13% PEG 20,000, 100-400 mM NaCl, 100 mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11drop100 (mM)
21dropEDTA1 (mM)
31dropdithiothreitol1 (mM)
41drop1 (mM)
51dropHEPES20 (mM)
61dropprotein5-8 (mg/ml)
71reservoir100-400 (mM)
81reservoirPEG200009-13 (%)
91reservoirMES100 (mM)

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PDB entries from 2024-05-01

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