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6YXZ

Structure and activity of the GH20 beta-N-beta-N-acetylhexosaminidase from Bifidobacterium bifidum

This is a non-PDB format compatible entry.
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsDIAMOND BEAMLINE I04
Synchrotron siteDiamond
BeamlineI04
Temperature [K]100
Detector technologyPIXEL
Collection date2019-05-18
DetectorDECTRIS EIGER2 XE 16M
Wavelength(s)0.9795
Spacegroup nameP 21 21 21
Unit cell lengths56.566, 126.750, 152.710
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution63.380 - 1.750
Rwork0.160
R-free0.21970
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)generated by MrBUMP
RMSD bond length0.009
RMSD bond angle1.511
Data reduction softwareDIALS
Data scaling softwareAimless
Phasing softwareSHELXDE
Refinement softwareREFMAC (5.8.0258)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]63.3801.780
High resolution limit [Å]1.7501.750
Rmerge1.654
Rpim0.969
Number of reflections1115195474
<I/σ(I)>91.1
Completeness [%]100.0100
Redundancy7.47.4
CC(1/2)0.9970.610
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.529321.6 mg/mL of purified protein in the buffer of tris 25 mM pH 8.0 and NaCl 200 mM is mixed with PEG 3350 23%, 0.1 M bis-tris propane PH 6.5 and 0.2 M NaBr at 1:1 ratio.

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