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1K7C

Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]263
Detector technologyIMAGE PLATE
Collection date1997-06-15
DetectorMARRESEARCH
Wavelength(s)1.1024
Spacegroup nameP 21 21 21
Unit cell lengths52.170, 56.920, 71.690
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution38.000

*

- 1.120
R-factor0.103

*

Rwork0.103
R-free0.13900

*

Structure solution methodMIR
Starting model (for MR)1deo
RMSD bond length0.015
RMSD bond angle0.031
Data scaling softwareSCALEPACK
Phasing softwareMLPHARE
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]38.0001.140
High resolution limit [Å]1.1201.120
Rmerge0.060

*

0.370
Total number of observations644629

*

Number of reflections80624

*

Completeness [%]97.782.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5298Molgaard, A., (1998) Acta Crystallogr., Sect.D, 54, 1026.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoir1.4 (M)or 1.4M (NH4)2SO4
21reservoirsodium acetate0.1 (M)

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