1F5V

STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 1
Unit cell lengths	51.560, 52.860, 52.830
Unit cell angles	75.79, 60.71, 61.17

Refinement procedure

Resolution	7.000 - 1.700
R-factor	0.189 *
Rwork	0.189
R-free	0.20600
RMSD bond length	0.011
RMSD bond angle	21.918 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall
High resolution limit [Å]	1.700 *
Rmerge	0.033 *
Number of reflections	41935 *
Completeness [%]	91.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5	5 *	PEG 6000, MES, sodium hydroxide, PEG 400, dioxane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 281.0K
1	Vapor diffusion, hanging drop *	6.5	5 *	PEG 6000, MES, sodium hydroxide, PEG 400, dioxane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 281.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	22.5 (%)
2	1	reservoir	PEG400	2-15 (%)
3	1	reservoir	MES	100 (mM)
4	1	drop	protein	9 (mg/ml)