6H9F

Structure of glutamate mutase reconstituted with bishomo-coenzyme B12

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	CCD
Collection date	2000-04-01
Detector	MARRESEARCH
Wavelength(s)	0.9080
Spacegroup name	P 1 21 1
Unit cell lengths	63.749, 112.286, 108.010
Unit cell angles	90.00, 95.71, 90.00

Refinement procedure

Resolution	35.350 - 2.100
R-factor	0.1599
Rwork	0.158
R-free	0.20290
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ccw
RMSD bond length	0.007
RMSD bond angle	0.868
Data reduction software	MOSFLM
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.400	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.207	0.642
Rmeas	0.241	0.749
Rpim	0.123	0.383
Number of reflections	88205	33437
<I/σ(I)>	6.7	2.3
Completeness [%]	99.9	99.8
Redundancy	3.8	3.8
CC(1/2)	0.974	0.679

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	293	6% (w/v) PEG-4000, 0.1 M DL-tartrate, pH=4.5, 2 mM CdCl2