4P9G

Structure of the 2,4'-dihydroxyacetophenone dioxygenase from Alcaligenes sp.

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	2013-04-03
Detector	MAR CCD 165 mm
Wavelength(s)	1.072
Spacegroup name	P 65 2 2
Unit cell lengths	82.557, 82.557, 114.008
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	71.500 - 2.200
R-factor	0.17564
Rwork	0.173
R-free	0.21758
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ebr 2oq1 3bal 3cjx
RMSD bond length	0.019
RMSD bond angle	2.008
Phasing software	BALBES
Refinement software	REFMAC (5.8.0069)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	57.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.136	0.619
Number of reflections	10549
<I/σ(I)>	12.6	3.1
Completeness [%]	86.3	49.4
Redundancy	9.8	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	Protein solution: protein concentration = 5 mg/ml in 50 mM Tris pH 7.5, 100 mM NaCl, 1 mM beta-mercaptoethanol. Chymotrypsin was added in a 1:50 mass-ratio prior to setting up hanging-drop crystallisation trials. Well solution: 10 % w/v PEG 1k and 10 % PEG 10k (Molecular Dimensions Structure Screen 2, condition 46).