4KFA

Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with mg and zoledronate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I02
Synchrotron site	Diamond
Beamline	I02
Temperature [K]	100
Detector technology	CCD
Collection date	2009-05-15
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9796
Spacegroup name	P 41 21 2
Unit cell lengths	111.200, 111.200, 67.090
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	37.070 - 1.980
R-factor	0.182
Rwork	0.181
R-free	0.20130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3cp6
RMSD bond length	0.010
RMSD bond angle	0.870
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASES
Refinement software	BUSTER (2.10.0)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	37.070	2.180	2.090
High resolution limit [Å]	1.980	2.100	1.980
Rmerge	0.118	0.618	0.049
Number of reflections	29896
<I/σ(I)>	10.7	1.9	34.3
Completeness [%]	100.0	93.4	97.7
Redundancy	8	7.7	8.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	0.2M NH4CL, 20% PEG 6000, 10% Ethylene glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K