3OC9

Crystal structure of putative UDP-N-acetylglucosamine pyrophosphorylase from Entamoeba histolytica

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2010-07-31
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97946
Spacegroup name	P 21 21 21
Unit cell lengths	76.520, 77.540, 86.870
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.1909
Rwork	0.189
R-free	0.22660
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jv1 molecule A residues 68-407
RMSD bond length	0.018
RMSD bond angle	1.300
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.046	0.020	0.529
Number of reflections	48589	625	3573
<I/σ(I)>	30.45	72.7	4.4
Completeness [%]	100.0	99.5	100
Redundancy	9.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	96.3 mg/mL of EnhiA.01126.b.A1 PS00631 3C cleaved against JCSG+ condition H9, 0.2 M lithium sulfate, 0.1 M BisTris pH 5.5, 25% PEG 3350 with 15% ethylene glycol as cryo-protectant, crystal tracking ID 216241h9, VAPOR DIFFUSION, SITTING DROP, temperature 289K