1OP0

Crystal Structure of AaV-SP-I, 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
Collection date	1999-07-06
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	49.415, 74.593, 82.419
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.100 * - 2.000
R-factor	0.181
Rwork	0.181
R-free	0.20800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bqy
RMSD bond length	0.005
RMSD bond angle	25.000 *
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]	50.000	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.123	0.478 *
Number of reflections	20865
Completeness [%]	98.1	85.4

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))