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1I4K

CRYSTAL STRUCTURE OF AN SM-LIKE PROTEIN (AF-SM1) FROM ARCHAEOGLOBUS FULGIDUS AT 2.5A RESOLUTION

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-04-14
DetectorMARRESEARCH
Wavelength(s)0.842
Spacegroup nameP 1 21 1
Unit cell lengths110.397, 64.563, 129.862
Unit cell angles90.00, 92.09, 90.00
Refinement procedure
Resolution20.000 - 2.500
R-factor0.207

*

Rwork0.207
R-free0.26400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)A seven membered ring of an Sm-like protein from Pyrococcus abyssii.
RMSD bond length0.008
RMSD bond angle1.500
Data scaling softwareXDS
Phasing softwareMOLREP
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.600
High resolution limit [Å]2.5002.500
Rmerge0.072

*

0.353

*

Total number of observations255898

*

Number of reflections63291
<I/σ(I)>14.13.5
Completeness [%]99.399.9
Redundancy4.043.34
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.320

*

PEG 6000, sodium citrate, pH 4.3, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein11 (mg/ml)
21reservoirPEG600012 (%)
31reservoirsodium citrate100 (mM)pH4.3

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PDB entries from 2024-05-15

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