1L6I

Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-02-08
Detector	MARRESEARCH
Wavelength(s)	1.2
Spacegroup name	P 21 21 21
Unit cell lengths	75.331, 105.937, 218.895
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.200
R-factor	0.2 *
Rwork	0.197
R-free	0.24300 *
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1l5v
RMSD bond length	0.021 *
RMSD bond angle	1.900 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	DM
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.190	0.360
Total number of observations	413101 *
Number of reflections	81626
<I/σ(I)>	8.4	2.5
Completeness [%]	91.4	87.4
Redundancy	5.1	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	291	PEG 4000, TRIS, Lithium Chloride, Glucose-1-phosphate, pH 8.5, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6.0 (mg/ml)
2	1	drop	Glc1P	100 (mM)
3	1	reservoir	PEG4000	27 (%(w/v))
4	1	reservoir		0.1 (M)
5	1	reservoir	Tris	0.1 (M)	pH8.5