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3CAZ

Crystal structure of a BAR protein from Galdieria sulphuraria

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-D
Synchrotron siteAPS
Beamline23-ID-D
Temperature [K]100
Detector technologyCCD
Collection date2007-08-18
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.96411
Spacegroup nameP 61 2 2
Unit cell lengths78.962, 78.962, 456.028
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution47.168 - 3.344
R-factor0.217
Rwork0.215
R-free0.25200
Structure solution methodSAD
RMSD bond length0.006
RMSD bond angle0.904
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]47.16847.1683.470
High resolution limit [Å]3.3447.2203.344
Rmerge0.0850.0460.858
Number of reflections13119
<I/σ(I)>11.4251.622
Completeness [%]98.394.198.2
Redundancy12.811.89.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP277Protein solution (10 mg/mL Se-Met protein, 0.05 M Sodium chloride, 0.0003 M TCEP, 0.005 M Bis-Tris pH 7.0) mixed in a 1:1 ratio with the Well solution (27% MPD, 0.12 M Magnesium chloride, 0.1 M MES/Acetate pH 5.5), VAPOR DIFFUSION, HANGING DROP, temperature 277K

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