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2NQT

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution

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 nameC 1 2 1
Unit cell lengths140.877, 77.983, 87.884
Unit cell angles90.00, 127.38, 90.00
Refinement procedure
Resolution40.660 - 1.580
R-factor0.16422
Rwork0.163
R-free0.18531
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.009
RMSD bond angle1.237
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.640
High resolution limit [Å]1.5801.580
Number of reflections93633
<I/σ(I)>16.873.34
Completeness [%]90.360.2
Redundancy2.41.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.529325% PEG 3350, 0.1M HEPES, 0.2M Ammonium acetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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