4GS1

Crystal structure of DyP-type peroxidase from Thermobifida cellulosilytica

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	2012-07-15
Detector	RAYONIX MX-300
Wavelength(s)	0.97857
Spacegroup name	P 21 21 21
Unit cell lengths	87.680, 91.190, 110.550
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.914 - 1.700
R-factor	0.1471
Rwork	0.146
R-free	0.17380
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2gvk
RMSD bond length	0.006
RMSD bond angle	1.109
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.8_1066)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	20.000	20.000	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge		0.053	0.477
Number of reflections	97818	1981	13894
<I/σ(I)>	12.93	26.14	2.6
Completeness [%]	99.9	94.2	99.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	Protein solution was at 15 mg/mL, containing 20 mM Tris and 150 mM NaCl. Mother liqueur contained 170 mM (NH4)2SO4, 25.5% PEG 4,000 and 15% (w/v) glycerol, pH 7.5, vapor diffusion, sitting drop, temperature 277K