5WIR

Structure of the TRF1-TERB1 interface

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2016-04-22
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 64
Unit cell lengths	161.720, 161.720, 45.170
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.685 - 2.100
R-factor	0.1806
Rwork	0.179
R-free	0.21040
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3bqo
RMSD bond length	0.009
RMSD bond angle	0.993
Data reduction software	iMOSFLM
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.940	2.160
High resolution limit [Å]	2.100	2.100
Rmerge	0.118	0.533
Rpim	0.036	0.166
Number of reflections	39942
<I/σ(I)>	12.4	3.8
Completeness [%]	100.0	100
Redundancy	11.6	11.3
CC(1/2)	0.998	0.939

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	TRF1-TRFH and TERB1-TBM were mixed in a 1:5 molar ratio and crystal screens set up using 0.3 microliter protein solution and 0.3 microliter reservoir solution in a sitting drop format. Diffracting crystals were obtained in 0.1 M Tris-Cl (pH 8.5) and 30% PEG 300. Crystals were cryoprotected in the crystallization solution plus 10% PEG 400 and harvested in liquid nitrogen.