1GKD

MMP9 active site mutant-inhibitor complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	298
Detector technology	CCD
Collection date	2000-08-22
Detector	ADSC CCD
Spacegroup name	P 41 21 2
Unit cell lengths	56.523, 56.523, 263.761
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.300 - 2.100
Rwork	0.212
R-free	0.25600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	WILD-TYPE MMP-9 STRUCTURE (1GKC)
RMSD bond length	0.006
RMSD bond angle	23.000 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNX (2000)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.300	2.270
High resolution limit [Å]	2.100	2.100
Rmerge	0.147	0.385
Total number of observations	50609 *
Number of reflections	18276	2038 *
<I/σ(I)>	7.5	2.5
Completeness [%]	71.2 *	40.4 *
Redundancy	2.7	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5 *	15 *	PROTEIN SOLUTION (4MG/ML IN 20MM TRIS-HCL PH 7.5, 50MM NACL) WAS INCUBATED WITH 5MM INHIBITOR FOR 30MINS PRIOR TO SETTING UP CRYSTALLISATION TRIALS. THE CRYSTALLISATION DROPS CONTAINED A 1:1 MIXTURE OF COMPLEX SOLUTION AND RESERVOIR BUFFER (2.6 - 2.8 M NACL, 0.1 M HEPES PH 9.0).

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	4 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH7.5
3	1	drop		50 (mM)
4	1	drop	inhibitor	5.0 (mM)
5	1	reservoir		2.6-2.8 (M)
6	1	reservoir	HEPES	0.1 (M)	pH9.0