1JCR

CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE NON-SUBSTRATE TETRAPEPTIDE INHIBITOR CVFM AND FARNESYL DIPHOSPHATE SUBSTRATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-05-19
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 61
Unit cell lengths	171.225, 171.225, 69.332
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.000
R-factor	0.166
Rwork	0.166
R-free	0.20600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1d8d
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.020
High resolution limit [Å]	2.000	2.000
Rmerge	0.054 *	0.397 *
Total number of observations	277944 *
Number of reflections	78430 *
<I/σ(I)>	26.4	2.48
Completeness [%]	100.0 *	99.8
Redundancy	3.5	3.28

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.7	17 *	PEG 8000, Ammonium Acetate, DTT, Tris-HCl, pH 5.7, VAPOR DIFFUSION, HANGING DROP at 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	14 (%(w/v))
2	1	reservoir	ammonium acetate	200-600 (mM)
3	1	reservoir	dithiothreitol	20 (mM)