3MLL

Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4C
Synchrotron site	NSLS
Beamline	X4C
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-11-17
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	68.131, 69.138, 79.936
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	52.000 - 3.250
R-factor	0.24438
Rwork	0.242
R-free	0.29753
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1phm
RMSD bond length	0.007
RMSD bond angle	1.057
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.000	3.370
High resolution limit [Å]	3.250	3.250
Number of reflections	6287
<I/σ(I)>	25.3	2.2
Completeness [%]	99.1	91.9
Redundancy	5.7	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	Crystallization: 0.1-0.5mM CuSO4, 1.25 mM NiCl2, 100mM sodium cacodylate pH=5.5, 3mM sodium azide and 5% glycerol. The crystal was first soaked in 5mM ascorbic acid and then soaked in 40mM NaN3 (with 5mM ascorbic acid) for 6 hours at RT., VAPOR DIFFUSION, HANGING DROP, temperature 293K