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1PEV

Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X9A
Synchrotron siteNSLS
BeamlineX9A
Temperature [K]100
Detector technologyCCD
Collection date2001-10-14
DetectorADSC QUANTUM 4
Wavelength(s)0.98
Spacegroup nameP 1 21 1
Unit cell lengths40.660, 90.817, 76.983
Unit cell angles90.00, 94.06, 90.00
Refinement procedure
Resolution21.700

*

- 2.000
R-factor0.197
Rwork0.197
R-free0.23400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1nr0
RMSD bond length0.008
RMSD bond angle26.900

*

Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]21.700

*

2.070
High resolution limit [Å]2.0002.000
Rmerge0.0580.256
Number of reflections36740
Completeness [%]97.087.8

*

Redundancy2.972.48
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6

*

289PEG 8000, MES, manganese chloride, glycerol, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein3-4 (mg/ml)
21reservoirMES0.1 (M)
31reservoirPEG800020 (%)
41reservoir10 (mM)
51reservoirglycerol3 (%)pH6.0

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