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1M6N

Crystal structure of the SecA translocation ATPase from Bacillus subtilis

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID2
Synchrotron siteESRF
BeamlineID2
Temperature [K]100
Detector technologyAREA DETECTOR
Collection date1997-12-15
DetectorMARRESEARCH
Wavelength(s)0.986
Spacegroup nameP 31 1 2
Unit cell lengths130.833, 130.833, 150.350
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution45.240 - 2.700
R-factor0.22
Rwork0.220
R-free0.30400

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Structure solution methodMIR
RMSD bond length0.013
RMSD bond angle1.740

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareDM
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.000

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2.750
High resolution limit [Å]2.7002.700
Rmerge0.078

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Number of reflections40372
<I/σ(I)>18.92.14
Completeness [%]99.6

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0.973
Redundancy6.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7299Weinkauf, S., (2001) Acta Crystallogr., Sect.D, 57, 559.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15-20 (mg/ml)
21dropammonium sulfate300 (mM)
31dropdithiothreitol1 (mM)
41dropBES20 (mM)pH7.0
51reservoirammonium sulfate46-52 (%sat)
61reservoirglycerol28-32 (%(v/v))
71reservoirBES20-100 (mM)pH7.0

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PDB entries from 2024-05-15

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