9DR5

Crystal structure of Catechol 1,2-dioxygenase from Burkholderia multivorans (Zinc bound, P1 form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-07-14
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 1
Unit cell lengths	84.970, 86.270, 110.161
Unit cell angles	106.04, 96.74, 113.15

Refinement procedure

Resolution	51.990 - 1.710
R-factor	0.1522
Rwork	0.151
R-free	0.18300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.862
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.21rc1_5156: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	102.350	1.750
High resolution limit [Å]	1.710	1.710
Rmerge	0.066	0.709
Rmeas	0.078	0.836
Rpim	0.041	0.439
Total number of observations	987993	72882
Number of reflections	278593	20527
<I/σ(I)>	10.1	1.7
Completeness [%]	96.4
Redundancy	3.5	3.6
CC(1/2)	0.998	0.632

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	291	20% 3350, 0.5M NaCl, 0.1M NaAc 4.6, BumuA.00107.d.A2.PW32075 at 21.7 mg/mL. plate 14238 well B2 drop 2. Protein was prepared in the presence if ZnCl2. Puck: PSL-1607, Cryo: 20% (v/v) PEG 200 + 80% (v/v) crystallant