1ND1

Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities.

Experimental procedure

Experimental method	LAUE
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE D03B-MX1
Synchrotron site	LNLS
Beamline	D03B-MX1
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	2002-07-23
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	38.425, 60.364, 86.257
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.310 - 1.900 *
R-factor	0.191
Rwork	0.191
R-free	0.21590 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB_ID 1QUA
RMSD bond length	0.010
RMSD bond angle	2.257 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	500.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.072 *
Total number of observations	49843 *
Number of reflections	14941 *
Completeness [%]	92.1	51.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9	298	PEG 20000, dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG20000	10 (%)	pH9.0
3	1	reservoir	dioxane	2 (%(v/v))