1REO

L-amino acid oxidase from Agkistrodon halys pallas

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BSRF BEAMLINE 3W1A
Synchrotron site	BSRF
Beamline	3W1A
Temperature [K]	300
Wavelength(s)	0.8883
Spacegroup name	I 21 3
Unit cell lengths	169.310, 169.310, 169.310
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.310
R-factor	0.194
Rwork	0.194
R-free	0.21600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f8r
RMSD bond length	0.006
RMSD bond angle	22.400 *
Data reduction software	AUTOMAR
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.310 *	2.310 *
Rmerge	0.054 *	0.383 *
Total number of observations	247448 *
Number of reflections	34867
Completeness [%]	98.2 *	99.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	300	ammonium sulfate, citrate soldium, nikel sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	44 (mg/ml)	in double-distilled water
2	1	reservoir	sodium citrate	0.1 (M)	pH5.6
3	1	reservoir	ammonium sulfate	2 (M)
4	1	reservoir		10 (mM)