1LI1

The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	100
Detector technology	CCD
Collection date	2001-10-27
Detector	MARRESEARCH
Wavelength(s)	1.05
Spacegroup name	H 3
Unit cell lengths	234.589, 234.589, 99.492
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.950 - 1.900
R-factor	0.182
Rwork	0.182
R-free	0.20200
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	25.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.950	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.058 *	0.300 *
Total number of observations	441349 *
Number of reflections	155867
Completeness [%]	96.9	97.6
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.1	293	MES, sodium acetate, pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop		20 (mM)
3	1	reservoir	MES-NaOH	0.1 (M)
4	1	reservoir	sodium acetate	3.2-3.6 (M)	pH7.1-7.5