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1MJI

DETAILED ANALYSIS OF RNA-PROTEIN INTERACTIONS WITHIN THE BACTERIAL RIBOSOMAL PROTEIN L5/5S RRNA COMPLEX

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-1
Synchrotron siteESRF
BeamlineID14-1
Temperature [K]100
Wavelength(s)0.9680
Spacegroup nameP 1 21 1
Unit cell lengths51.890, 99.600, 65.730
Unit cell angles90.00, 100.05, 90.00
Refinement procedure
Resolution15.000

*

- 2.500
R-factor0.21
Rwork0.210
R-free0.28800
Structure solution methodMAD
RMSD bond length0.007
RMSD bond angle1.310

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.590
High resolution limit [Å]2.5002.500
Rmerge0.0670.186
Number of reflections22852

*

1908

*

<I/σ(I)>13.23.3
Completeness [%]99.9

*

84.1
Redundancy3.02

*

3.0

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.5298sodium cacodylate, magnesium acetate, potassium chlorate, PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111sodium cacodylate
211magnesium acetate
311potassium chlorate
411PEG 8000
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein2 (mg/ml)
21dropsodium cacodylate50 (mM)pH6.5
31dropmagnesium acetate100 (mM)
41drop50 (mM)
51dropPEG800010 (%)
61reservoirsodium cacodylate50 (mM)pH6.5
71reservoirmagnesium acetate100 (mM)
81reservoir200 (mM)
91reservoirPEG800010 (%)

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PDB entries from 2024-07-03

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