1FT2

CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	96
Detector technology	IMAGE PLATE
Collection date	1998-04-27
Detector	RIGAKU
Spacegroup name	P 65
Unit cell lengths	166.660, 166.660, 98.820
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.000 - 3.400
R-factor	0.219
Rwork	0.219
R-free	0.26800
Structure solution method	MOLECULAR REPLACEMENT USING 1FT1 COORDINATES
Starting model (for MR)	1ft1
RMSD bond length	0.009
RMSD bond angle	21.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	3.440
High resolution limit [Å]	3.400	3.400
Rmerge	0.053	0.199
Total number of observations	42609 *
Number of reflections	17125
<I/σ(I)>	15	2.7
Completeness [%]	79.4	58.1 *
Redundancy	2.5	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.7 *	17 *	HANGING DROP, PROTEIN CONCENTRATION OF 16MG/ML IN 20 MM KCL, 10UM ZNCL, 10MM DTT, 20MM TRIS PH 7.7, 0.12% OCTYL-BETA-D-GLUCOPYRANOSIDE, AND 1MM FARNESYL DIPHOSPHATE; RESERVOIR SOLUTION OF 15% PEG 8000, 200MM AMMONIUM ACETATE, PH 7.0, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	20 (mM)
2	1	drop	octyl-beta-D-glucopyranoside	0.6 (%(w/v))
3	1	drop	FPP	1 (mM)
4	1	drop	FTase	0.14 (mM)
5	1	reservoir	PEG8000	15 (%(w/v))
6	1	reservoir	ammonium acetate	200 (mM)
7	1	reservoir	imidazole-malic acid	100 (mM)
8	1	reservoir	dithiothreitol	10 (mM)