1LFD

CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	92
Collection date	1997-09
Spacegroup name	P 21 21 21
Unit cell lengths	75.648, 78.256, 87.313
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.100
R-factor	0.206
Rwork	0.206
R-free	0.28200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lxd 6q21
RMSD bond length	0.005 *
RMSD bond angle	1.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	X-PLOR (3.85)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.061	0.061
Total number of observations	129387 *
Number of reflections	30504
<I/σ(I)>	24.5	5.7
Completeness [%]	98.3	97.5
Redundancy	4.2	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *		pH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	50 (mM)
2	1	drop	dithiothreitol	10 (mM)
3	1	drop		5 (mM)
4	1	drop	protein	15 (mg/ml)
5	1	reservoir	PEG8000	7-10 (%)
6	1	reservoir	MES	100 (mM)
7	1	reservoir	ammonium sulfate	200 (mM)
8	1	reservoir	dithiothreitol	4 (mM)
9	1	reservoir		5 (mM)