5CVA

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a2a1 of type I collagen

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2014-07-15
Detector	NOIR-1
Wavelength(s)	0.97879, 0.97901, 0.96337
Spacegroup name	P 1 21 1
Unit cell lengths	52.410, 63.980, 65.370
Unit cell angles	90.00, 112.75, 90.00

Refinement procedure

Resolution	48.333 - 2.098
R-factor	0.2382
Rwork	0.234
R-free	0.27850
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	0.986
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.140
High resolution limit [Å]	2.098	5.700	2.100
Rmerge	0.094	0.076	0.286
Rmeas	0.102	0.082	0.332
Rpim	0.039	0.031	0.163
Total number of observations	131621
Number of reflections	21132
<I/σ(I)>	14.7
Completeness [%]	89.9	99.8	48.9
Redundancy	6.2	7.1	3.5
CC(1/2)		0.998	0.898

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	295	0.1 M BisTris, 16% PEG MME 5,000