6C7S

Structure of Rifampicin Monooxygenase with Product Bound

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	CMOS
Collection date	2016-02-19
Detector	RDI CMOS_8M
Wavelength(s)	1
Spacegroup name	P 65 2 2
Unit cell lengths	81.877, 81.877, 286.205
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	63.536 - 2.100
R-factor	0.202
Rwork	0.200
R-free	0.24110
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5kow
RMSD bond length	0.002
RMSD bond angle	0.684
Data reduction software	XDS
Data scaling software	Aimless (0.5.32)
Phasing software	PHASER
Refinement software	PHENIX (1.10_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	63.540	63.540	2.160
High resolution limit [Å]	2.100	8.910	2.100
Rmerge	0.091	0.031	0.691
Rmeas	0.094	0.032	0.720
Rpim	0.021	0.008	0.192
Total number of observations	636732
Number of reflections	33890	579	2345
<I/σ(I)>	25.3
Completeness [%]	98.6	99.3	86.6
Redundancy	18.8	16.2	13.3
CC(1/2)	0.999	0.999	0.843

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	The reservoir contained 24% (w/v) PEG 3350, 200 mM magnesium chloride. The protein stock solution included 5 mM RIF, 100 mM NADPH and 100 mM dithionite.