2GHE

Conformational mobility in the active site of a heme peroxidase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2006-01-15
Detector	ADSC QUANTUM 4
Spacegroup name	P 42 21 2
Unit cell lengths	82.003, 82.003, 75.012
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.050 - 1.750
R-factor	0.18167
Rwork	0.180
R-free	0.22034
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.011
RMSD bond angle	1.188
Data reduction software	MOSFLM
Refinement software	REFMAC (5.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.990	1.840
High resolution limit [Å]	1.750	1.750
Rmerge	0.059
Number of reflections	26381
<I/σ(I)>	30.6	11.6
Completeness [%]	99.8	100
Redundancy	13.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.3	273	0.1 M HEPES, pH 8.3, 2.25 M Lithium Sulphate, VAPOR DIFFUSION, SITTING DROP, temperature 273K