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2I3A

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.3.1
Synchrotron siteALS
Beamline8.3.1
Temperature [K]100
Detector technologyCCD
Collection date2006-04-13
DetectorADSC QUANTUM 210
Wavelength(s)1.11587
Spacegroup nameP 21 21 21
Unit cell lengths89.695, 104.031, 138.435
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution48.680 - 2.150
R-factor0.16429
Rwork0.161
R-free0.22450
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.020
RMSD bond angle1.798
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.230
High resolution limit [Å]2.1502.150
Number of reflections69868
Completeness [%]98.992.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.529520% PEG MME 5000, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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