1E77

COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-10-22
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	129.800, 44.300, 91.200
Unit cell angles	90.00, 105.10, 90.00

Refinement procedure

Resolution	25.000 - 2.690
R-factor	0.18
Rwork	0.180
R-free	0.28500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	REFINED COORDINATES OF APO-ENZYME IN THE SAME SPACEGROUP
RMSD bond length	0.006
RMSD bond angle	22.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.900	2.790
High resolution limit [Å]	2.690	2.690
Rmerge	0.112 *	0.331 *
Total number of observations	38922 *
Number of reflections	13462
<I/σ(I)>	9	3.3
Completeness [%]	94.6	93.1
Redundancy	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *		HANGING DROP VAPOUR DIFFUSION, 2+2 MICROLITER DROPS. THE WELL BUFFER: 21% W/V PEG 400 IN 0.1M HEPES-NAOH, PH 7.8 WITH 0.2M CALCIUM CHLORIDE. THE PROTEIN AT 7MG/ML, WITH 20MM GLUCOSE 6-PHOSPHATE AND 10MM BENZAMIDE ADENINE DINUCLEOTIDE (BAD).

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	15 (mg/ml)
2	1	drop	Tris-HCl	0.1 (M)
3	1	drop	NAD+	29 (mM)
4	1	reservoir	PEG400	20 (%(v/v))
5	1	reservoir	HEPES/NaOH	0.1 (M)
6	1	reservoir		0.2 (M)