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3LMA

Crystal structure of the stage V sporulation protein AD (SpoVAD) from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR6.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X4C
Synchrotron siteNSLS
BeamlineX4C
Temperature [K]100
Detector technologyCCD
Collection date2010-01-25
DetectorMAR CCD 165 mm
Wavelength(s)0.97916
Spacegroup nameP 1 21 1
Unit cell lengths64.957, 83.059, 103.662
Unit cell angles90.00, 101.01, 90.00
Refinement procedure
Resolution38.939 - 1.993
R-factor0.1703
Rwork0.168
R-free0.21090
Structure solution methodSAD
RMSD bond length0.008
RMSD bond angle1.378
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHELXDE
Refinement softwarePHENIX ((phenix.refine: 1.5_2))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.070
High resolution limit [Å]1.9932.000
Rmerge0.0750.201
Number of reflections142035
<I/σ(I)>20.14.53
Completeness [%]97.484.2
Redundancy3.42.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1icrobatch crystallization under paraffin oil7.529140% PEG 1000, 0.1M ammonium phosphate, 0.1M HEPES, pH 7.5, icrobatch crystallization under paraffin oil, temperature 291K

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