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1O7D

The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
DetectorADSC CCD
Spacegroup nameP 61 2 2
Unit cell lengths117.880, 117.880, 582.040
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.700
R-factor0.257
Rwork0.257
R-free0.28900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1hty
RMSD bond length0.010
RMSD bond angle24.400

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.760
High resolution limit [Å]2.7002.700
Rmerge0.0900.540
Number of reflections60071
<I/σ(I)>15.92.1
Completeness [%]89.4

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77.7

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Redundancy33.0

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Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

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7.5PROTEIN 9 MG/ML IN 20 MM TRIS-CL, PH 7.5, 150 MM NACL MIXED 1:1 WITH 100 MM TRIS-CL, PH 7.5, 50 % SAT. (NH4)2SO4
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein9 (mg/ml)
21dropTris-HCl20 (mM)pH7.5
31drop150 (mM)
41reservoirammonium sulfate50 (%sat)
51reservoirTris-HCl100 (mM)pH7.5

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PDB entries from 2024-05-15

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