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1QO8

The structure of the open conformation of a flavocytochrome c3 fumarate reductase

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-04-15
DetectorMARRESEARCH
Wavelength(s)0.8469, 1.033, 1.739, 1.741
Spacegroup nameP 21 21 21
Unit cell lengths71.770, 109.690, 227.320
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.150
R-factor0.225

*

Rwork0.225
R-free0.28100
Structure solution methodMAD
RMSD bond length0.015
RMSD bond angle0.013
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.190
High resolution limit [Å]2.1502.150
Rmerge0.038

*

0.274

*

Total number of observations1428311

*

Number of reflections97968
Completeness [%]93.4

*

91.4
Redundancy14.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5

*

Bamford, V., (1999) Acta Crystallogr.,Sect., D55, 1222.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10-15 (mg/ml)
21dropsodium HEPES50 (mM)
31drop100 (mM)
41reservoirPEG100006-15 (%(w/v))
51reservoirsodium MES

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PDB entries from 2024-05-15

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