5C5U

The crystal structure of viral collagen prolyl hydroxylase vCPH from Paramecium Bursaria Chlorella virus-1 - Truncated Construct

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04-1
Synchrotron site	Diamond
Beamline	I04-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-04-27
Detector	DECTRIS PILATUS 2M
Wavelength(s)	0.92
Spacegroup name	P 1 21 1
Unit cell lengths	33.770, 157.670, 41.010
Unit cell angles	90.00, 90.02, 90.00

Refinement procedure

Resolution	28.400 - 1.700
R-factor	0.163
Rwork	0.156
R-free	0.20240
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2jig
RMSD bond length	0.005
RMSD bond angle	0.872
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (dev_1977)

Data quality characteristics

	Overall
Low resolution limit [Å]	28.400
High resolution limit [Å]	1.700
Number of reflections	44328
<I/σ(I)>	10.4
Completeness [%]	94.6
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	vCPH was concentrated to 30 mg/ml in 100 mM HEPES, pH 7.5, before being supplemented with 1.1 mM MnCl2. Crystals of vCPH were grown by sitting drop vapour diffusion, incubated at 4 C and arose from a reservoir solution containing 0.1 M [Imidazole; MES monohydrate (acid)], 0.1 M amino acids [0.2 M L-Na-Glutamate; 0.2 M Alanine (racemic); 0.2 M Glycine; 0.2M Lysine HCL (racemic); 0.2 M Serine (racemic)], 30 % PEGMME 550 PEG 20K pH 6.5 [Morpheus HT96 condition H1, Molecular Dimensions].