2H39

Crystal Structure of an ADP-Glucose Phosphorylase from Arabidopsis thaliana with bound ADP-Glucose

Replaces:  2GDK

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	BRUKER AXS MICROSTAR
Temperature [K]	100
Detector technology	CCD
Collection date	2005-09-10
Detector	BRUKER PROTEUM-R
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	61.318, 95.454, 110.504
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.727 - 2.230
Rwork	0.176
R-free	0.24340
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	: 1Z84
RMSD bond length	0.017
RMSD bond angle	1.664
Data scaling software	SAINT
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.730	47.730	2.250
High resolution limit [Å]	2.230	6.250	2.230
Rmerge	0.191	0.093	0.676
Number of reflections	32389
<I/σ(I)>	11.28	26.04	2.92
Completeness [%]	100.0	99.6	99.9
Redundancy	11.78	18.07	7.34

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	10 MG/ML PROTEIN, 20% PEG 2000, 0.2M SODIUM CHLORIDE, 0.10M MES-ACETATE, vapor diffusion, hanging drop, temperature 293K