4NG6

The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 41 21 2
Unit cell lengths	111.740, 111.740, 66.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.980 - 2.350
R-factor	0.1803
Rwork	0.178
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3cp6
RMSD bond length	0.010
RMSD bond angle	0.980
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	BUSTER (2.10.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.980	2.490
High resolution limit [Å]	2.350	2.350
Rmerge	0.161
Number of reflections	17960
<I/σ(I)>	10.3
Completeness [%]	99.2	95.7
Redundancy	8.6

Crystallization Conditions

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