5SXW

Crystal structure of the E198A variant of catalase-peroxidase KatG of Burkholderia pseudomallei

Replaces:  3N3R

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	2009-12-09
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97949
Spacegroup name	P 21 21 21
Unit cell lengths	100.340, 116.020, 174.710
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.600
R-factor	0.1443
Rwork	0.143
R-free	0.16910
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1MWV
RMSD bond length	0.033
RMSD bond angle	2.738
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0151)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	96.650	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.084	0.550
Number of reflections	267341
<I/σ(I)>	11.9	2.8
Completeness [%]	100.0	100
Redundancy	5.9	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	16-20% PEG 4000, 20% MPD, 25 mM NaCl, 0.1 M sodium citrate pH 5.6