1LD7

Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 66

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-02-21
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 61
Unit cell lengths	178.725, 178.725, 64.549
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 2.000
R-factor	0.194 *
Rwork	0.195
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jcq
RMSD bond length	0.006
RMSD bond angle	1.181 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	2.130
High resolution limit [Å]	2.000	2.000
Rmerge	0.090 *	0.247 *
Total number of observations	211060 *
Number of reflections	75509 *
<I/σ(I)>	9.3
Completeness [%]	94.7 *	60 *
Redundancy	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	17 *	PEG8K, NH4OAc, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium acetate	200-400 (mM)
2	1	reservoir	PEG8000	12-14 (%)	pH5.3-5.5
3	1	drop	protein	10 (mg/ml)