1RQR

Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2003-03-08
Detector	MARRESEARCH
Wavelength(s)	0.9786
Spacegroup name	C 2 2 21
Unit cell lengths	76.184, 129.923, 183.872
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	53.000 * - 2.700 *
R-factor	0.17627
Rwork	0.173
R-free	0.23900 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014 *
RMSD bond angle	1.340 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.000 *	2.740
High resolution limit [Å]	2.700 *	2.670
Rmerge	0.064 *	0.130 *
Number of reflections	26303 *
<I/σ(I)>	3	5.4
Completeness [%]	97.0 *	81 *
Redundancy	6.3	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.8 *	293	Dong, C., (2003) Acta Crystallogr.,Sect.D, 59, 2292. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG1000	22 (%)
2	1	reservoir	phosphate-citrate	0.1 (M)	pH4.2
3	1	reservoir		0.2 (M)
4	1	drop	Tris-HCl	25 (mM)	pH7.8
5	1	drop	protein	5 (mg/ml)