4MBG
Crystal structure of Aspergillus fumigatus protein farnesyltransferase binary complex with farnesyldiphosphate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-08 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.252, 90.793, 83.138 |
Unit cell angles | 90.00, 110.87, 90.00 |
Refinement procedure
Resolution | 23.960 - 1.740 |
R-factor | 0.124 |
Rwork | 0.122 |
R-free | 0.16400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HOMOLOGY MODEL OF ASPERGILLUS FUMIGATUS PROTEIN FARNESYLTRANSFERASE GENERATED USING PHYRE |
RMSD bond length | 0.011 |
RMSD bond angle | 1.231 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASES |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.740 |
Number of reflections | 89198 |
Completeness [%] | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 290 | 4-10 % PEG6000, 600-800 mM LiCl, and 100 mM HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |