5VQA

Structure of human TRIP13, ATP-bound form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2015-10-19
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97918
Spacegroup name	P 65
Unit cell lengths	98.479, 98.479, 120.979
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.339 - 2.540
R-factor	0.1993
Rwork	0.197
R-free	0.24080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4xgu
RMSD bond length	0.007
RMSD bond angle	0.986
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.10_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	121.030	2.660
High resolution limit [Å]	2.540	2.540
Rmerge	0.093	1.767
Rpim	0.043	0.821
Number of reflections	22993	2231
<I/σ(I)>	16.4	0.9
Completeness [%]	97.9	83.1
Redundancy	5.7	5.3
CC(1/2)	0.999	0.516

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	0.1 M Tris-HCl pH 8.5, 0.2 M KCl, 10% pentaerythritol propoxylate, 5 mM MgCl2, 1 mM ATP, cryoprotected with 10% glycerol and 12% additional pentaerythritol propoxylate