1E2O

CATALYTIC DOMAIN FROM DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

Experimental procedure

Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1994-03
Detector	MARRESEARCH
Spacegroup name	F 4 3 2
Unit cell lengths	222.800, 222.800, 222.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 3.000
R-factor	0.205
Rwork	0.205
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1eaa
RMSD bond length	0.010
RMSD bond angle	24.700 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((ROTAVATA)
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.160
High resolution limit [Å]	3.000	3.000
Rmerge	0.046 *	0.145 *
Number of reflections	9906
<I/σ(I)>	13	4.9
Completeness [%]	98.5	100
Redundancy	4.1	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.3 *		PROTEIN WAS CRYSTALLIZED FROM 1.2M AMMONIUM SULFATE, 1% ETHANOL, 50 MM POTASSIUM PHOSPHATE, PH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	potassium phosphate	50 (mM)
3	1	drop	dithiothreitol	1 (mM)
4	1	drop	EDTA	1 (mM)
5	1	drop	benzamidine	1 (mM)
6	1	reservoir	ammonium sulfate	1.2 (M)
7	1	reservoir	ethanol	1 (%(v/v))