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1L4I

Crystal Structure of the Periplasmic Chaperone SfaE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX31
Temperature [K]288
Detector technologyAREA DETECTOR
Collection date1995-06-02
DetectorMARRESEARCH
Wavelength(s)0.9204
Spacegroup nameP 21 21 21
Unit cell lengths53.500, 84.240, 97.340
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 2.200
R-factor0.19

*

Rwork0.190
R-free0.24400
Structure solution methodMIR
RMSD bond length0.014
RMSD bond angle0.037
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.240
High resolution limit [Å]2.2002.200
Rmerge0.068

*

0.267
Total number of observations151034

*

Number of reflections22920
<I/σ(I)>8.9
Completeness [%]99.998.8
Redundancy6.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5

*

298PEG 4000, sodium citrate, ammonium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropHEPES20 (mM)
31reservoirPEG400030 (%)
41reservoirTris-HCl0.1 (M)pH8.5
51reservoirsodium acetate0.2 (M)

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