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1AD2

RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE

Experimental procedure
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1995-11
DetectorMARRESEARCH
Spacegroup nameP 21 21 2
Unit cell lengths76.100, 61.400, 46.100
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 1.900
R-factor0.203
Rwork0.203
R-free0.27000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)NAT L1
RMSD bond length0.013
RMSD bond angle25.140

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Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]12.000
High resolution limit [Å]1.8001.800
Rmerge0.0590.320
Total number of observations116835

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Number of reflections24181
<I/σ(I)>8.5
Completeness [%]98.898.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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10

*

Nikonov, S., (1996) EMBO J., 15, 1350.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein12-15 (mg/ml)
21dropglycine-NaOH50 (mM)
31dropmethane pentanediol5 (%(v/v))
41dropammonium sulfate30 (%sat)
51reservoirammonium sulfate60 (%sat)
61reservoirmethane pentanediol7 (%)

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