2YLS

SNAPSHOTS OF ENZYMATIC BAEYER-VILLIGER CATALYSIS: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION: REDUCED ENZYME BOUND TO NADP

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	P 32 2 1
Unit cell lengths	107.920, 107.920, 106.830
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	42.810 - 2.260
R-factor	0.18932
Rwork	0.187
R-free	0.23549
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ylr
RMSD bond length	0.022
RMSD bond angle	1.881
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.400
High resolution limit [Å]	2.260	2.260
Rmerge	0.090	0.300
Number of reflections	34153
<I/σ(I)>	8.7	3.4
Completeness [%]	99.6	98.8
Redundancy	3	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	277	BY VAPOR-DIFFUSION AT 4 DEGREES C USING 1-3 MICROL OF PROTEIN SOLUTIONS (18 MG/ML IN 0.5 MICROM FAD AND 4 MM NADP, 50 MM TRIS/HCL PH 7.5) MIXED WITH EQUAL VOLUMES OF RESERVOIR CONTAINING 40% W/V PEG4000, 100 MM MES/HCL PH 6.5, AND 100 MM NACL.