1L5V

Crystal Structure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate

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	1999-12-10
Detector	MARRESEARCH
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	74.833, 105.277, 218.617
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.182 *
Rwork	0.180
R-free	0.22000 *
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1qm5
RMSD bond length	0.020
RMSD bond angle	1.800 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	DM
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.150	0.550
Total number of observations	423852 *
Number of reflections	110577
<I/σ(I)>	7.2	1.8
Completeness [%]	94.7	82.4
Redundancy	3.8	2.8

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