2JEV

Crystal structure of human spermine,spermidine acetyltransferase in complex with a bisubstrate analog (N1-acetylspermine-S-CoA).

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	194
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IV
Spacegroup name	P 43
Unit cell lengths	46.729, 46.729, 191.792
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.950 - 2.300
R-factor	0.227
Rwork	0.224
R-free	0.27500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2f5i
RMSD bond length	0.011
RMSD bond angle	1.354
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.500	2.420
High resolution limit [Å]	2.300	2.300
Rmerge	0.040	0.230
Number of reflections	17959
<I/σ(I)>	20.2	4.3
Completeness [%]	98.5	93.9
Redundancy	3.8	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5		PROTEIN AT 15MG/ML IN 20 MM TRIS PH 8.0 CONTAINING 1 MM DTT, 0.1 MM EDTA, 4MM N1-ACETYLSPERMINE-S-COA. CRYSTALLIZED BY HANGING DROP VAPOUR DIFFUSION WITH 3-4 M NACL, 200 MM K/NA TARTRATE, 100 MM TRIS-HCL PH 7-8, 50 MM MGCL2