4IRV

Structure of the Helicobacter pylori CagA Oncogene Bound to the Human Tumor Suppressor Apoptosis-stimulating Protein of p53-2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Detector technology	CCD
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97869
Spacegroup name	C 1 2 1
Unit cell lengths	118.641, 120.239, 100.659
Unit cell angles	90.00, 115.64, 90.00

Refinement procedure

Resolution	90.750 - 2.040
R-factor	0.19148
Rwork	0.189
R-free	0.23410
Structure solution method	SAD
RMSD bond length	0.019
RMSD bond angle	1.909
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall
Low resolution limit [Å]	90.750
High resolution limit [Å]	2.040
Number of reflections	80050

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5		Crystals were grown by vapor diffusion at 25 degrees C using hanging drops formed from mixing a 2ul of the protein complex with 2ul of an equilibration buffer (21% polyethylene glycol (PEG) molecular weight 4 kDa, 200 mM Li2 SO4 , and 100 mM Tris pH 8.5) and 0.6ul of the Silver Bullets additive 43 (Hampton Research HR2-996-43). Significantly higher quality crystals were obtained from selenomethionine-substituted protein complexes and they were used for the final refinement, VAPOR DIFFUSION, HANGING DROP