1L6J

Crystal structure of human matrix metalloproteinase MMP9 (gelatinase B).

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Detector technology	CCD
Detector	BRANDEIS
Wavelength(s)	1.271632, 1.209997, 1.272917
Spacegroup name	P 65
Unit cell lengths	123.685, 123.685, 89.937
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 2.500
Rwork	0.187
R-free	0.22300 *
Structure solution method	MAD
Starting model (for MR)	1ck7
RMSD bond length	0.012 *
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.077	0.194
Number of reflections	47453 *	3904 *
<I/σ(I)>	11.5	2.4
Completeness [%]	89.1	73.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.2	293	sodium chloride, Tris, HEPES, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12.8 (mg/ml)
2	1	drop	Tris	20 (mM)	pH8.2
3	1	drop		100 (mM)
4	1	reservoir		4.3 (M)
5	1	reservoir	HEPES	0.1 (M)	pH7.0