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1OHA

Acetylglutamate kinase from Escherichia coli complexed with MgADP and N-acetyl-L-glutamate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
Collection date2000-05-10
DetectorMARRESEARCH
Spacegroup nameC 2 2 21
Unit cell lengths60.126, 71.792, 107.175
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.430 - 1.900
R-factor0.2
Rwork0.200
R-free0.22950
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gs5
RMSD bond length0.005
RMSD bond angle1.500
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]19.4302.000
High resolution limit [Å]1.9001.900
Rmerge0.0680.469
Total number of observations154986

*

Number of reflections18636
<I/σ(I)>7.31.3
Completeness [%]99.999.6
Redundancy8.36
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

4.627-29% POLYETHYLENE GLYCOL MONOMETHYL ETHER 2K, SODIUM ACETATE 0.1M PH 4.6 AMMONIUM SULFATE 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 citrate0.25-0.4 (M)
41dropprotein10 (mg/ml)

219869

PDB entries from 2024-05-15

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