1JCI

Stabilization of the Engineered Cation-binding Loop in Cytochrome c Peroxidase (CcP)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	116
Detector technology	IMAGE PLATE
Collection date	2000-01-31
Detector	RIGAKU RAXIS IV
Spacegroup name	P 21 21 21
Unit cell lengths	106.680, 75.340, 51.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.900
R-factor	0.1582 *
Rwork	0.158
R-free	0.19910
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	calcium binding CcP
RMSD bond length	0.005
RMSD bond angle	2.252
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.088	0.347
Total number of observations	315272 *
Number of reflections	33299
<I/σ(I)>		4.1969112
Completeness [%]	99.4 *	99.5
Redundancy	9.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6	277	Sundaramoorthy, M., (1991) J.Am.Chem.Soc., 113, 7755. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	10 (mg/ml)
2	1	2	potassium phosphate	0.05 (M)	pH6.0
3	1	2	MPD	25 (%)