1SLN

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842

Experimental procedure

Source type	SEALED TUBE
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1990-12-01
Detector	SIEMENS
Spacegroup name	P 31 2 1
Unit cell lengths	47.230, 47.230, 150.850
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.270
R-factor	0.2263
Rwork	0.226
R-free	0.29900
RMSD bond length	0.009
RMSD bond angle	24.200 *
Data reduction software	XENGEN
Data scaling software	XENGEN
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000	2.410
High resolution limit [Å]	2.270	2.260
Rmerge	0.060	0.189 *
Number of reflections	8311
<I/σ(I)>	11.9	4.03
Completeness [%]	88.9	60.9
Redundancy	2.79	1.71

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.54		HANGING DROP VAPOR DIFFUSION. 1.5 MICROLITER DROPS OF ENZYME:INHIBITOR SOLUTION (9 MG/ML ENZYME, 1.5 MILLIMOLAR INHIBITOR, 5.0 MILLIMOLAR CALCIUM CHLORIDE, 0.02% SODIUM AZIDE, 20 MILLIMOLAR TRIS HYDROCHLORIDE, PH 7.5) WERE MIXED WITH AN EQUAL VOLUME OF RESERVOIR BUFFER (10% PEG-6000, 15% SATURATED AMMONIUM ACETATE 0.02% SODIUM AZIDE, 0.1 M CACODYLATE, PH 5.54) AND INCUBATED AT ROOM TEMPERATURE., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	9 (mg/ml)
2	1	drop	I	1.5 (mM)
3	1	drop		5.0 (mM)
4	1	drop		0.02 (%)
5	1	drop	Tris-HCl	20 (mM)
6	1	reservoir	PEG6000	10 (%)
7	1	reservoir		15 (%sat)
8	1	reservoir		0.02 (%)
9	1	reservoir	cacodylate	0.1 (M)