2CAH

STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH

Replaces:  1CAF

Experimental procedure

Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6A
Synchrotron site	Photon Factory
Beamline	BL-6A
Detector technology	FILM
Collection date	1994
Spacegroup name	P 62 2 2
Unit cell lengths	112.360, 112.360, 249.140
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.700
R-factor	0.196
Rwork	0.196
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PMC WITH NADPH AT 3.1 A RESOLUTION
RMSD bond length	0.015
RMSD bond angle	3.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	2.823	2.820
High resolution limit [Å]	2.700	2.700
Rmerge	0.049
Number of reflections	24337
Completeness [%]	92.0	92.4
Redundancy	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	4-5 *	Jouve, H.M., (1991) J.Mol.Biol., 221, 1075. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	27 (mg/ml)
2	1	drop	Tris-HCl	100 (mM)
3	1	drop	glycerol	2.5 (%(v/v))
4	1	drop	ammonium sulfate	1 (M)
5	1	drop		25 (mM)
6	1	reservoir	ammonium sulfate	2 (M)
7	1	reservoir		50 (mM)
8	1	reservoir	Tris-HCl	100 (mM)