1SLM

CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1993-03-04
Detector	RIGAKU
Spacegroup name	F 2 2 2
Unit cell lengths	111.040, 145.560, 76.750
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.900
R-factor	0.2185
Rwork	0.218
R-free	0.25600
RMSD bond length	0.009
RMSD bond angle	23.200 *
Data reduction software	R-AXIS
Data scaling software	R-AXIS
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.045
Number of reflections	24169
<I/σ(I)>	8.29	1.45
Completeness [%]	98.2	95.8
Redundancy	2.82

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.8	277	HANGING DROP VAPOR DIFFUSION. 2.0 MICROLITER DROPS OF PROENZYME SOLUTION (10 MG/ML PROTEIN, 5.0 MILLIMOLAR CALCIUM CHLORIDE, 50 MICROMOLAR ZINC ACETATE, 0.02% SODIUM AZIDE, 20 MILLIMOLAR MES, PH 6.5, 0.02 MOLE INHIBITOR PER MOLE PROENZYME) WERE MIXED WITH AN EQUAL VOLUME OF RESERVOIR BUFFER (14% PEG-6000, 5% SATURATED SODIUM CITRATE, 0.02% SODIUM AZIDE, 0.1 M CACODYLATE, PH 5.8) AND INCUBATED AT 4 DEGREES CENTIGRADE., vapor diffusion - hanging drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop		5 (mM)
3	1	drop		0.05 (mM)
4	1	drop		0.02 (%)
5	1	drop	MES	20 (mM)
6	1	reservoir	PEG6000	14 (%)
7	1	reservoir	Na-citrate	5 (%sat)
8	1	reservoir	cacodylate	100 (mM)