1MQF

Compound I from Proteus mirabilis catalase

Replaces:  2CAF

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1995-10-13
Detector	MARRESEARCH
Wavelength(s)	0.98
Spacegroup name	P 62 2 2
Unit cell lengths	110.000, 110.000, 250.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 * - 2.500
R-factor	0.196
Rwork	0.196
R-free	0.23400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	24.300 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.044 *	0.104 *
Total number of observations	138931 *
Number of reflections	30822 *
<I/σ(I)>	10.7	6.7
Completeness [%]	98.3 *	97.1 *
Redundancy	4.5	4.1

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)