1MNI

ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT

Experimental procedure

Spacegroup name	I 1 21 1
Unit cell lengths	124.490, 42.280, 92.270
Unit cell angles	90.00, 92.62, 90.00

Refinement procedure

Resolution	10.000 - 2.070
R-factor	0.175
R-free	0.22700 *
RMSD bond length	0.017
RMSD bond angle	0.055
Refinement software	PROLSQ

Data quality characteristics

	Overall	Outer shell
High resolution limit [Å]	2.070 *	2.070 *
Rmerge	0.042 *	0.211 *
Number of reflections	26337 *
Completeness [%]	88.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.1 *	15 *	Dodson, G.(1988). Protein. Eng., 2, 233-237. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	reservoir	sodium phosphate	50 (mM)
3	1	reservoir	ammonium sulfate	80 (%)