1GR3

Structure of the human collagen X NC1 trimer

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	293
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	78.360, 78.360, 141.036
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.186
Rwork	0.186
R-free	0.19900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c28
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.076	0.385
Number of reflections	11537
<I/σ(I)>	13.5	4.1
Completeness [%]	99.9	100
Redundancy	4.7	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	9.5 *		1.6 M MGSO4, 0.1 M MES PH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	glycine-NaOH	100 (mM)	pH9.5
2	1	drop		100 (mM)
3	1	drop	CHAPS	0.5 (%(w/v))
4	1	drop	protein	10 (mg/ml)
5	1	reservoir		1.2-1.6 (M)
6	1	reservoir	MES- NaOH	100 (mM)	pH6.5