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1OA3

Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
Collection date2000-04-29
DetectorADSC CCD
Spacegroup nameP 1 21 1
Unit cell lengths62.490, 77.547, 83.410
Unit cell angles90.00, 98.46, 90.00
Refinement procedure
Resolution29.000 - 1.700
R-factor0.1927
Rwork0.192
R-free0.21700

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Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1h8v
RMSD bond length0.011

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RMSD bond angle1.300

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.730
High resolution limit [Å]1.7001.700
Rmerge0.097

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0.126

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Total number of observations346287

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Number of reflections85680
<I/σ(I)>145.7
Completeness [%]98.984.6
Redundancy4.0

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Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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620-24

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pH 6.00
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoircacodylate200 (mM)pH6.0
21reservoirammonium acetate200 (mM)
31reservoirPEG2000MME10-30 (%(w/w))
41dropprotein15 (mg/ml)

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PDB entries from 2024-05-15

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