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1H9X

Cytochrome cd1 Nitrite Reductase, reduced form

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-06-06
DetectorMARRESEARCH
Spacegroup nameP 43 21 2
Unit cell lengths127.970, 127.970, 264.130
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 2.100
R-factor0.216

*

Rwork0.216
R-free0.24100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1aof D1 DOMAIN DIMER
RMSD bond length0.009

*

RMSD bond angle2.100

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.180
High resolution limit [Å]2.1002.100
Rmerge0.0770.224
Number of reflections126324
<I/σ(I)>17.63.9
Completeness [%]99.799.6
Redundancy3.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP9HANGING DROP USING 2.1 M AMMONIUM SULPHATE AND 100 MM CHES PH 7.0 1 MM ASCORMBATE AND 2.5 UM PMS FROM REDUCTION OF PROTEIN WAS ALSO PRESENT IN CRYSTALLISATION.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15-20 (mg/ml)
21dropascorbate2 (mM)
31dropphenazine methosulphate0.005 (mM)
41reservoirammonium sulfate2.0 (M)
51reservoirCHES100 (mM)

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