1AHP

OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1995-02
Detector	MAR scanner 300 mm plate
Spacegroup name	C 1 2 1
Unit cell lengths	173.200, 112.400, 121.700
Unit cell angles	90.00, 119.70, 90.00

Refinement procedure

Resolution	10.000 - 3.000
R-factor	0.232
Rwork	0.232
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MALP NATIVE STRUCTURE
RMSD bond length	0.008
RMSD bond angle	24.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.080
High resolution limit [Å]	3.000	3.000
Rmerge	0.140	0.318
Total number of observations	52324 *
Number of reflections	33108
<I/σ(I)>	5.4	1.9
Completeness [%]	81.7	80.3
Redundancy	1.6	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.4	16 *	0.1M NATARTRATE, PH 6.4, 24% PEG 3350, 1MM SODIUM AZIDE, 16 DEG CELCIUS, 50MM MALTOHEXAOSE STOCK, 16.5MG/ML PROTEIN STOCK, HANGING DROPS 1MICRO LITRE WELL & 0.5 MICRO LITRE MALTOHEXAOSE 0.5 MICRO LITRE PROTEIN, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3350	20-24 (%)
10	1	protein	sodium tartrate	0.05 (M)
2	1	reservoir	sodium azide	1 (mM)
3	1	reservoir	sodium chloride	0.5-0.8 (M)
4	1	reservoir	sodium tartrate	0.1 (M)
5	1	protein	MalP N133A		0.005ml
6	1	protein	maltohexaose	10-12.5 (mM)
7	1	protein	PEG3350	10-12 (%)
8	1	protein	sodium azide	0.5 (mM)
9	1	protein	sodium chloride	0.25-0.4 (M)