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2IIH

Crystal structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from thermus theromophilus HB8 (H32 form)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-BM
Synchrotron siteAPS
Beamline22-BM
Temperature [K]100
Detector technologyCCD
Collection date2006-08-24
DetectorMARMOSAIC 225 mm CCD
Wavelength(s)0.97243
Spacegroup nameH 3 2
Unit cell lengths106.573, 106.573, 59.251
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution23.500 - 1.750
R-factor0.196
Rwork0.196
R-free0.21700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2ide
RMSD bond length0.004
RMSD bond angle1.400
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.810
High resolution limit [Å]1.7501.750
Rmerge0.0960.175
Number of reflections13115
Completeness [%]99.9100
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP52930.1M Na Acetate, 1.0M Ammonium H2 phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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