1LWO

Crystal structure of rabbit muscle glycogen phosphorylase a in complex with a potential hypoglycaemic drug at 2.0 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	2000-03-03
Wavelength(s)	1.05
Spacegroup name	P 43 21 2
Unit cell lengths	128.648, 128.648, 116.521
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.400 * - 2.000
R-factor	0.207
Rwork	0.207
R-free	0.23500
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1lwn
RMSD bond length	0.007
RMSD bond angle	1.260 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.078	0.658
Total number of observations	343075 *
Number of reflections	64780 *	3121 *
<I/σ(I)>	13.2	3.3
Completeness [%]	97.5	95.7
Redundancy	4.8	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	SMALL TUBES	6.7	298	Oikonomakos, N.G., (1999) Protein Sci., 8, 1930. *