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1HCM

Cytochrome cd1 Nitrite Reductase, oxidised from from tetragonal crystals

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-10-05
DetectorMARRESEARCH
Spacegroup nameP 43 21 2
Unit cell lengths128.305, 128.305, 264.825
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 2.500
R-factor0.226

*

Rwork0.226
R-free0.25800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1h9x
RMSD bond length0.012

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RMSD bond angle1.700

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.590
High resolution limit [Å]2.5002.500
Rmerge0.0620.280
Number of reflections74676
<I/σ(I)>17.63.9
Completeness [%]98.191.2
Redundancy3.12.8

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP9HANGING DROP USING 2.1 M AMMONIUM SULPHATE AND 100 MM CHES PH 7.0 1 MM ASCORBATE AND 2.5 UM PMS FROM REDUCTION OF PROTEIN WAS ALSO PRESENT IN CRYSTALLISATION. CRYSTALS WERE GROWN UNDER STRICTLY ANAEROBIC CONDITIONS. THE ENZYME WAS OXIDISED IN THE CRYSTAL BY ALLOWING AIR TO DIFFUSE INTO THE DROP
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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PDB entries from 2024-04-24

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