1Q7C

The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	100
Detector technology	CCD
Collection date	2003-02-05
Detector	ENRAF-NONIUS
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	75.857, 95.857, 131.617
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	65.800 - 2.500
R-factor	0.2187
Rwork	0.215
R-free	0.25200 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.170 *
Data reduction software	SAINT
Data scaling software	SAINT
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	65.800	2.610
High resolution limit [Å]	2.500	2.500
Rmerge	0.057 *	0.174 *
Total number of observations	172466 *
Number of reflections	17095	2163 *
Completeness [%]	100.0	100
Redundancy	10.1 *	7.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6 *		VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	20 (mM)	pH7.6
2	1	drop		50 (mM)
3	1	drop	dithiothreitol	1 (mM)
4	1	drop	EDTA	1 (mM)
5	1	drop	protein	5 (mg/ml)
6	1	reservoir	PEG1000	20 (%)
7	1	reservoir	calcium acetate	0.2 (M)
8	1	reservoir	Tris-HCl	0.1 (M)	pH9.0