1I01

CRYSTAL STRUCTURE OF BETA-KETOACYL [ACYL CARRIER PROTEIN] REDUCTASE FROM E. COLI.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	CCD
Collection date	2000-04-12
Detector	BRANDEIS - B4
Wavelength(s)	0.97938, 0.95373
Spacegroup name	P 1 21 1
Unit cell lengths	61.700, 120.100, 131.100
Unit cell angles	90.00, 90.50, 90.00

Refinement procedure

Resolution	29.000 * - 2.600
R-factor	0.228 *
Rwork	0.228
R-free	0.25000
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.200
Data reduction software	MARMAD
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.740
High resolution limit [Å]	2.600	2.600
Rmerge	0.072	0.093
Number of reflections	56511
<I/σ(I)>	6.5
Completeness [%]	96.3	96.3
Redundancy	6.3	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.9 *	291	PEG 10000, Hepes, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	20 (mM)	pH7.9
2	1	drop	dithiothreitol	1 (mM)
3	1	drop	EDTA	100 (mM)
4	1	reservoir	PEG10000	20 (%)
5	1	reservoir	HEPES	100 (mM)	pH8.5