1L5W

Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose

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	CCD
Collection date	2001-03-24
Detector	MARRESEARCH
Wavelength(s)	1.2
Spacegroup name	P 21 21 21
Unit cell lengths	74.508, 105.236, 217.361
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.187 *
Rwork	0.186
R-free	0.21600 *
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1l5v
RMSD bond length	0.018
RMSD bond angle	1.700 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASES
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	17.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.180	0.610
Total number of observations	1056617 *
Number of reflections	134845
<I/σ(I)>	11	2
Completeness [%]	85.0	73.6
Redundancy	7.8	5.2

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, VAPOR DIFFUSION, HANGING DROP, 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