1LWN

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 X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1998-06-06
Wavelength(s)	0.9058
Spacegroup name	P 43 21 2
Unit cell lengths	128.283, 128.283, 116.881
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.800 * - 2.000
R-factor	0.179
Rwork	0.179
R-free	0.21800
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	glycogen phosphorylase a room temperature model provided by Prof. R.J.Fletterick
RMSD bond length	0.007
RMSD bond angle	1.310 *
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]	15.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.067	0.490
Total number of observations	453933 *
Number of reflections	65781 *	3229 *
<I/σ(I)>	16.7	4.1
Completeness [%]	99.3	99.2
Redundancy	5.9	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	SMALL TUBES	6.7	295	Oikonomakos, N.G., (1999) Protein Sci., 8, 1930. *