1FS4

Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1996-04-03
Detector	NICOLET
Spacegroup name	P 43 21 2
Unit cell lengths	128.500, 128.500, 116.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.500 - 2.380
R-factor	0.177 *
Rwork	0.177
R-free	0.22400 *
Structure solution method	DIFFERENCE FOURIER METHODS
RMSD bond length	0.008
RMSD bond angle	1.400
Data reduction software	X-GEN
Data scaling software	XDS
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.500	2.490
High resolution limit [Å]	2.380	2.380
Rmerge	0.076
Total number of observations	145498 *
Number of reflections	32187 *
Completeness [%]	82.0

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6.7	16 *	Oikonomakos, N.G., (1985) Biochim.Biophys.Acta., 832, 248. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	phosphorylase b	27.5 (mg/ml)
2	1	1	IMP	1.1 (mM)
3	1	1	spermine	1.1 (mM)
4	1	1	Bes	10 (mM)
5	1	1	dithiothreitol	2.9 (mM)
6	1	1	EDTA	0.1 (mM)