2E3X

Crystal structure of Russell's viper venom metalloproteinase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	90
Detector technology	CCD
Collection date	2006-03-26
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	70.350, 91.730, 152.930
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.600 - 2.910
Rwork	0.218
R-free	0.27300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qua 2dw0 1j34
RMSD bond length	0.005
RMSD bond angle	1.160
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP (in CCP4)
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.000
High resolution limit [Å]	2.900	2.900
Rmerge	0.069	0.212
Number of reflections	20716
<I/σ(I)>	17	7
Completeness [%]	96.4	79.5
Redundancy	6.3	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Droplets were prepared by mixing 1l of protein solution and 1l of reservoir solution (0.1M calcium acetate, 0.1M sodium cacodylate, 10% PEG8000, pH 6.5) supplemented with one fifth volume of 10% PEG3350 as an additive and were equilibrated, typically, for one week against 1ml of reservoir solution., VAPOR DIFFUSION, SITTING DROP, temperature 293K