5ENU

Crystal structure of an alkyl hyroperoxide reductase from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2015-10-23
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	P 1 21 1
Unit cell lengths	53.340, 37.010, 75.360
Unit cell angles	90.00, 110.08, 90.00

Refinement procedure

Resolution	50.000 - 1.350
R-factor	0.1357
Rwork	0.135
R-free	0.17080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ixrA
RMSD bond length	0.007
RMSD bond angle	0.896
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((dev_2210))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.390
High resolution limit [Å]	1.350	6.040	1.350
Rmerge	0.049	0.030	0.431
Rmeas	0.056	0.034	0.506
Total number of observations	260972
Number of reflections	60081	694	4383
<I/σ(I)>	17.24	36.1	3.02
Completeness [%]	98.2	92.9	96.9
Redundancy	4.34		3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	MORPHEUS B4: 12.5% PEG1000, 12.5% PEG3350, 12.5% MPD, 100mM MES/imidazole pH6.5, 30mM NaF, 30mM NaBr, 30mM, NaI; BuamA.01056.a.B1.PS02485 at 17mg/mL; Direct cryo; tray 266491b4; puck gry8-1