3D11

Crystal Structures of the Nipah G Attachment Glycoprotein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Collection date	2007-08-18
Wavelength(s)	1.5498
Spacegroup name	P 21 3
Unit cell lengths	130.161, 130.161, 130.161
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.245 - 2.306
Rwork	0.228
R-free	0.25700
RMSD bond length	0.005
RMSD bond angle	0.757
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXS
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	2.380
High resolution limit [Å]	2.300	4.950	2.300
Rmerge	0.086	0.060	0.357
Number of reflections	55607
<I/σ(I)>	12.7
Completeness [%]	88.5	99.5	42.6
Redundancy	3.3	3.7	1.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.8	298	PEG 3350, KI, pH 6.8, vapor diffusion, hanging drop, temperature 298K