2OA1

Crystal Structure of RebH, a FAD-dependent halogenase from Lechevalieria aerocolonigenes, the L-Tryptophan with FAD complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2006-06-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97931
Spacegroup name	P 62
Unit cell lengths	114.492, 114.492, 231.935
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.952 - 2.150
R-factor	0.154
Rwork	0.152
R-free	0.19400
Structure solution method	2O9Z
Starting model (for MR)	apo form of same protein in same lattice
RMSD bond length	0.015
RMSD bond angle	1.412
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.576	49.580	2.200
High resolution limit [Å]	2.150	5.300	2.150
Rmerge	0.102	0.050	0.534
Number of reflections	92078
<I/σ(I)>	24.905		3.628
Completeness [%]	98.8	99.8	90.9
Redundancy	20.4	22.9	9.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	Protein Solution (18 mg/ml protein, 0.050 M sodium chloride, 0.010 M TRIS pH 8.0) mixed in a 1:1 ratio with the Well Solution (0.9 M K2HPO4, 0.5 M NaH2PO4) crystals soaked for 22 hours in solution of 0.6 M K2HPO4, 0.33 M NaH2PO4, ~0.005 M FAD, ~0.003 M L-tryptophan, 0.030 M NaCl, Cryoprotected with: well solution supplemented with up to 30% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K