1OP2

Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SEALED TUBE
Temperature [K]	298
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	119.430, 42.830, 44.940
Unit cell angles	90.00, 99.61, 90.00

Refinement procedure

Resolution	20.000 * - 2.100
R-factor	0.165
Rwork	0.165
R-free	0.21100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	25.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.150
High resolution limit [Å]	2.100	2.100
Rmerge	0.083 *	0.208 *
Number of reflections	12259
Completeness [%]	92.3	79.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.3 *	298	Zhu, Z., (2003) Acta Crystallogr., Sect.D, 59, 547. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)	in distilled water
2	1	reservoir	sodium cacodylate	30 (mM)	pH6.3
3	1	reservoir		27 (%(w/v))