2IGA

Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-05-20
Detector	NOIR-1
Spacegroup name	P 21 21 2
Unit cell lengths	110.678, 153.022, 96.389
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	52.700 - 1.950
Rwork	0.185
R-free	0.24500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f1x
RMSD bond length	0.018
RMSD bond angle	1.671
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	CCP4 ((MOLREP))
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.700	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.095	0.379
Number of reflections	105058
<I/σ(I)>	5.4	1.9
Completeness [%]	87.8	91.6
Redundancy	2.08	2.16

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.5	292	18% PEG8000, 0.2 M calcium acetate, 0.1 M sodium cacodylate. Prior to freezing in liquid nitrogen, crystals were sequentially transferred into mother liquor solutions containing 5, 10, 15, and then 20% glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K, pH 6.50