1D8D

CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	96
Detector technology	IMAGE PLATE
Collection date	1998-10-23
Detector	RIGAKU RAXIS IV
Spacegroup name	P 61
Unit cell lengths	170.919, 170.919, 69.284
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.000 - 2.000
R-factor	0.166
Rwork	0.164
R-free	0.20000
RMSD bond length	0.009
RMSD bond angle	21.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	2.020
High resolution limit [Å]	2.000	2.000
Rmerge	0.045	0.197
Total number of observations	320401 *
Number of reflections	76088
<I/σ(I)>	13.9
Completeness [%]	97.5	83.9
Redundancy	4.2	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.7	17 *	Peg 8000, ammonium acetate, DTT, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	12-16 (%(w/v))
2	1	reservoir	ammonium acetate	600 (mM)
3	1	reservoir	dithiothreitol	20 (mM)