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1VEW

MANGANESE SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU FR-C
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1996-07
DetectorRIGAKU
Spacegroup nameC 2 2 21
Unit cell lengths100.840, 108.910, 182.100
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000 - 2.100
R-factor0.186
Rwork0.188
R-free0.21800

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Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1mng
RMSD bond length0.010
RMSD bond angle15.600

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareTNT (5E)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.200
High resolution limit [Å]2.1002.100
Rmerge0.056

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0.191

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Total number of observations215051

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Number of reflections56890
<I/σ(I)>225.4
Completeness [%]96.877
Redundancy3.70.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5CRYSTALS WERE GROWN AT ROOM TEMPERATURE USING THE HANGING DROP METHOD. THE HANGING DROPS WERE SUSPENDED OVER 0.75ML OF WELL SOLUTION (16-30% PEG6000 AND 0.05M BICINE TITRATED TO PH8.5) AND CONSISTED OF 2UL OF WELL SOLUTION AND 2UL OF PROTEIN SOLUTION (MNSOD AT 12MG/ML IN WATER)., vapor diffusion - hanging drop
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6 (mg/ml)
21dropPEG60008-15 (%)
31dropbicine titrated0.025 (M)
41reservoirPEG600016-30 (%)
51reservoirbicine titrated0.05 (M)

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PDB entries from 2024-05-15

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