1MG3

MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-10-12
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	79.520, 188.372, 127.366
Unit cell angles	90.00, 98.84, 90.00

Refinement procedure

Resolution	50.000 - 2.400
Rwork	0.193
R-free	0.24600
Structure solution method	refined directly
Starting model (for MR)	mutant complex structure
RMSD bond length	0.006
RMSD bond angle	1.420 *
Data scaling software	SCALEPACK
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.093	0.246
Number of reflections	117875
<I/σ(I)>	9.3	2.2
Completeness [%]	81.3	50.7
Redundancy	3.7	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	295	phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	alphaF55A MADH	9.6 (mg/ml)
2	1	drop	amicyanin	2.9 (mg/ml)
3	1	drop	cytochrome c-551i	4.8 (mg/ml)
4	1	drop	sodium potassium phosphate	5 (mM)	pH5.0
5	1	reservoir	sodium potassium monobasic/dibasic phosphate buffer	2.4 (M)	pH5.0