6NL1

Structure of T. brucei MERS1 protein in its apo form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-12-04
Detector	DECTRIS PILATUS3 R CdTe 300K
Wavelength(s)	1.03
Spacegroup name	P 62 2 2
Unit cell lengths	122.160, 122.160, 170.101
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.975 - 2.297
R-factor	0.1889
Rwork	0.188
R-free	0.21310
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.017
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	PHENIX (1.6.4_486)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.975	2.356
High resolution limit [Å]	2.297	2.297
Rpim	0.028	0.278
Number of reflections	33970
<I/σ(I)>	13
Completeness [%]	99.7
Redundancy	5
CC(1/2)	0.997	0.879

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	1.6 M Magnesium sulphate, 0.1 M HEPES