4L9P

Crystal structure of Aspergillus fumigatus protein farnesyltransferase complexed with the FII analog, FPT-II, and the KCVVM peptide

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
Wavelength(s)	1.0
Spacegroup name	P 1 21 1
Unit cell lengths	63.236, 90.328, 83.007
Unit cell angles	90.00, 111.01, 90.00

Refinement procedure

Resolution	22.421 - 1.450
R-factor	0.1264
Rwork	0.125
R-free	0.15200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	> Homology model of A. fumigatus farnesyltransferase generated using PHYRE
RMSD bond length	0.019
RMSD bond angle	1.833
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	Outer shell
Low resolution limit [Å]	50.000	1.480
High resolution limit [Å]	1.450	1.450
Rmerge	0.069	0.591
Number of reflections	154808
<I/σ(I)>	36	2
Completeness [%]	99.1	82.8
Redundancy		5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	290	4-10% PEG6000, 600-800 mM LiCl, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K