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1OHB

Acetylglutamate kinase from Escherichia coli complexed with ADP and sulphate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]100
Detector technologyCCD
Collection date1999-11-01
DetectorMARRESEARCH
Spacegroup nameC 2 2 21
Unit cell lengths59.242, 71.449, 107.230
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution41.890 - 1.900
R-factor0.1948
Rwork0.195
R-free0.22110
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gs5
RMSD bond length0.005
RMSD bond angle1.200
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]41.8902.000
High resolution limit [Å]1.9001.900
Rmerge0.0750.357
Total number of observations100167

*

Number of reflections18284
<I/σ(I)>9.72.1
Completeness [%]99.9100
Redundancy5.55.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

4.627-29% POLYETHYLENE GLYCOL MONOMETHYL ETHER 2K, SODIUM ACETATE 0.1M PH 4.6 AMMONIUM SULPHATE 0.15-0.3 M
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG200027-29 (%(w/v))
21reservoirsodium acetate0.1 (M)pH4.6
31reservoirammonium citrate0.15-0.3 (M)
41dropprotein10 (mg/ml)

218853

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