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3LRK

Structure of alfa-galactosidase (MEL1) from Saccharomyces cerevisiae

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID23-1
Synchrotron siteESRF
BeamlineID23-1
Temperature [K]100
Detector technologyCCD
Collection date2009-02-07
DetectorADSC QUANTUM 315
Wavelength(s)0.979
Spacegroup nameP 4 21 2
Unit cell lengths101.243, 101.243, 111.521
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution111.520 - 1.950
R-factor0.205
Rwork0.204
R-free0.23400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1uas
RMSD bond length0.010
RMSD bond angle1.372
Data reduction softwareMOSFLM
Data scaling softwareSCALA (3.3.9)
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]111.5212.060
High resolution limit [Å]1.9501.950
Rmerge0.0670.457
Number of reflections42919
<I/σ(I)>7.61.7
Completeness [%]100.0100
Redundancy10.612
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP8.5295Deglycosylated sample. 19% PEG3350, 0.1 M BisTris, 0.2 M SCNK, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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