1RWB

Cooperative Effect of Two Surface Amino Acid Mutations (Q252L and E170K) of Glucose Dehydrogenase from Bacillus megaterium IWG3 for the stabilization of Oligomeric State

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2002-10-05
Detector	MARRESEARCH
Wavelength(s)	0.95
Spacegroup name	C 1 2 1
Unit cell lengths	118.500, 65.400, 118.000
Unit cell angles	90.00, 92.60, 90.00

Refinement procedure

Resolution	15.000 * - 2.000
R-factor	0.224
Rwork	0.224
R-free	0.26700
Structure solution method	Rigid Body
Starting model (for MR)	1gco
RMSD bond length	0.006
RMSD bond angle	22.300 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	1.920
High resolution limit [Å]	2.000 *	1.830
Rmerge	0.057 *	0.119 *
Total number of observations	193166 *
Number of reflections	61998 *
<I/σ(I)>	7	3.6
Completeness [%]	99.4	99.4
Redundancy	3.1 *	3.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.3 *	291	PEG 6000, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	10 (mg/ml)
2	1	reservoir	NAD+	4 (mM)
3	1	reservoir	sodium phosphate	50 (mM)	pH6.3