5KSK

Crystal structure of the catalase-peroxidase from B. pseudomallei treated with acetate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2015-10-09
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97949
Spacegroup name	P 21 21 21
Unit cell lengths	100.703, 115.480, 174.966
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.388 - 1.690
R-factor	0.1534
Rwork	0.152
R-free	0.17960
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1MWV
RMSD bond length	0.030
RMSD bond angle	2.396
Data reduction software	XDS
Data scaling software	SCALA (3.3.21)
Phasing software	REFMAC
Refinement software	REFMAC (5.8.0151)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	115.480	48.388	1.780
High resolution limit [Å]	1.690	5.340	1.690
Rmerge		0.052	0.484
Rmeas	0.081
Rpim	0.040
Total number of observations	843167
Number of reflections	225720
<I/σ(I)>	10.8	9.2	1.6
Completeness [%]	99.4	96.4	99.8
Redundancy	3.7	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.1	293	MPD, 0.1 M sodium citrate