2YLZ

SNAPSHOTS OF ENZYMATIC BAEYER-VILLIGER CATALYSIS: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION: Met446Gly MUTANT

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 210
Spacegroup name	I 2 2 2
Unit cell lengths	86.800, 115.910, 166.580
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.400 - 2.000
R-factor	0.19148
Rwork	0.190
R-free	0.22577
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1w4x
RMSD bond length	0.018
RMSD bond angle	1.607
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.090	0.420
Number of reflections	56991
<I/σ(I)>	11.6	4.8
Completeness [%]	100.0	100
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	CRYSTALS WERE GROWN AT 293 K BY THE VAPOUR DIFFUSION METHOD. HANGING DROPS WERE FORMED BY MIXING EQUAL VOLUMES OF 18 MG PROTEIN/ML IN 5 MM FAD AND 50 MM SODIUM PHOSPHATE PH 7.0, AND OF A WELL SOLUTION CONSISTING OF 1.5 M AMMONIUM SULPHATE AND 0.5 M LITHIUM CHLORIDE.