1I1J

STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-02-26
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9791, 0.9794, 1.0332
Spacegroup name	P 21 21 21
Unit cell lengths	47.534, 48.396, 87.774
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.850 - 1.390
R-factor	0.2087
Rwork	0.208
R-free	0.23100
Structure solution method	MAD
RMSD bond length	0.014
RMSD bond angle	0.031
Data reduction software	MOSFLM
Data scaling software	CCP4 ((TRUNCATE))
Phasing software	MLPHARE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.850	1.470
High resolution limit [Å]	1.390	1.390
Rmerge	0.062	0.240
Number of reflections	47146
<I/σ(I)>	16.8	3
Completeness [%]	99.4 *	91.5
Redundancy	6.6	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.55 *	295	PEG 8000, Tris, sodium chloride, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K
1	VAPOR DIFFUSION, HANGING DROP	4.55 *	295	PEG 8000, Tris, sodium chloride, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K
1	VAPOR DIFFUSION, HANGING DROP	4.55 *	295	PEG 8000, Tris, sodium chloride, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6.5 (mg/ml)
2	1	drop	acetate	10 (mM)
3	1	drop	azide	0.02 (%)
4	1	reservoir	Tris	100 (mM)
5	1	reservoir	PEG8000	8 (%)