2ICX

Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UTP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	BRUKER AXS MICROSTAR
Temperature [K]	100
Detector technology	CCD
Collection date	2006-05-02
Detector	BRUKER PROTEUM-R
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	187.683, 59.679, 89.813
Unit cell angles	90.00, 100.38, 90.00

Refinement procedure

Resolution	70.481 - 1.850
R-factor	0.195
Rwork	0.192
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1z90
RMSD bond length	0.016
RMSD bond angle	1.902
Data reduction software	SAINT
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]	70.481	70.481	1.900
High resolution limit [Å]	1.850	5.050	1.850
Rmerge	0.035	0.014	0.311
Number of reflections	83235
<I/σ(I)>	23.9	72.84	3.19
Completeness [%]	99.4	98.1	100
Redundancy	14.3		5.09

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	vapor diffusion, hanging drop with micro-seeding		273	Protein solution (10 mg/ml protein, 0.050 M sodium chloride, 0.0003 M TCEP, 0.005 M Tris PH 8.0) mixed in a 1:1 ratio with Well solution ( 28 % PEG 2K, 5% DMSO, 0.10 M MES/Acetate pH 5.5), crystals soaked in well solution supplemented with 0.002 M UTP, vapor diffusion, hanging drop with micro-seeding, temperature 273K