5EAU

5-EPI-ARISTOLOCHENE SYNTHASE FROM NICOTIANA TABACUM

Experimental procedure

Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	90
Detector technology	IMAGE PLATE
Collection date	1996-03
Detector	MARRESEARCH
Spacegroup name	P 41 21 2
Unit cell lengths	125.960, 125.960, 122.970
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.000 - 2.150
R-factor	0.242
Rwork	0.242
R-free	0.28700
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	5eas
RMSD bond length	0.006
RMSD bond angle	19.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.300	2.200
High resolution limit [Å]	2.160	2.150
Rmerge	0.076 *	0.469 *
Total number of observations	268076 *
Number of reflections	49688
<I/σ(I)>	8	2.7
Completeness [%]	91.5	70.3
Redundancy	5.4	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.9		PROTEIN WAS CRYSTALLIZED FROM 15% PEG 8000, 200 MM MG(OAC)2, 100 MM MOPSO PH 6.9, 1MM DTT; SOAKING SOLUTION FOR FREEZING ALSO INCLUDED 20% ETHYLENE GLYCOL.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	15 (%)
2	1	reservoir		200 (mM)
3	1	reservoir	MOPSO	100 (mM)
4	1	reservoir	dithiothreitol	1 (mM)