6AN3

Crystal structure of H172A-peptidylglycine alpha-hydroxylating monooxygenase (PHM) mutant soaked with peptide (no CuH bound, no peptide bound)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E DW
Temperature [K]	100
Detector technology	CCD
Collection date	2016-10-05
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	59.029, 66.847, 70.246
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.430 - 2.050
R-factor	0.2011
Rwork	0.197
R-free	0.28170
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1phm
RMSD bond length	0.016
RMSD bond angle	1.874
Data scaling software	SCALEPACK
Phasing software	REFMAC
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.090
High resolution limit [Å]	2.050	5.560	2.050
Rmerge	0.051	0.043	0.145
Rmeas	0.055	0.047	0.186
Rpim	0.022	0.020	0.114
Total number of observations	93871
Number of reflections	17232	1001	623
<I/σ(I)>	20.8
Completeness [%]	95.6	99.3	70.6
Redundancy	5.4	5.3	2
CC(1/2)		0.998	0.955

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8.5	293	19-24% PEG 4000, Tris HCL