1DD8

CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1996-06-15
Detector	RIGAKU RAXIS II
Spacegroup name	P 21 21 21
Unit cell lengths	59.620, 142.710, 213.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.300
Rwork	0.188
R-free	0.21900
RMSD bond length	0.013 *
RMSD bond angle	1.540 *
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]	30.000	30.000
High resolution limit [Å]	2.300	2.300
Rmerge	0.071	0.119
Number of reflections	76863
Completeness [%]	94.3	51
Redundancy	3.24	1.44

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	293	Olsen, J.G., (1995) Protein Pept. Lett., 1, 246. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	2.2 (M)
2	1	reservoir	PEG400	3 (%)
3	1	reservoir	HEPES-NaOH	0.1 (M)