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3O24

Crystal structure of the brevianamide F prenyltransferase FtmPT1 from Aspergillus fumigatus

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSLS BEAMLINE X06DA
Synchrotron siteSLS
BeamlineX06DA
Temperature [K]100
Detector technologyCCD
Collection date2009-09-26
DetectorMARMOSAIC 225 mm CCD
Wavelength(s)1.0000
Spacegroup nameP 41 21 2
Unit cell lengths82.850, 82.850, 121.760
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.500
R-factor0.189
Rwork0.186
R-free0.23650
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3i4z
RMSD bond length0.009
RMSD bond angle1.155
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwarePHASER
Refinement softwareREFMAC (5.5.0102)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.570
High resolution limit [Å]2.5002.500
Rmerge0.0720.254
Number of reflections14721
<I/σ(I)>13.795.48
Completeness [%]96.4100
Redundancy9.39.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.52981.3M ammonium sulfate, 0.2M lithium sulfate, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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