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1VP2

CRYSTAL STRUCTURE OF A PUTATIVE XANTHOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN HOMOLOG (TM0159) FROM THERMOTOGA MARITIMA AT 1.78 A RESOLUTION

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.1
Synchrotron siteALS
Beamline5.0.1
Temperature [K]100
Detector technologyCCD
Collection date2004-03-03
DetectorADSC
Spacegroup nameP 41 21 2
Unit cell lengths142.851, 142.851, 45.082
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution34.650 - 1.780
R-factor0.16777
Rwork0.166
R-free0.20473
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1v7r
RMSD bond length0.017
RMSD bond angle1.592
Data reduction softwareMOSFLM
Data scaling softwareSCALA (4.2))
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0001)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]34.6501.830
High resolution limit [Å]1.7801.780
Number of reflections37599
<I/σ(I)>12.61.8
Completeness [%]83.642.4
Redundancy4.43
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION,SITTING DROP,NANODROP2771.6M (NH4)2SO4, 0.1M NaCl, 0.1M HEPES pH 7.5, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K

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