5MMD

TMB-1. Structural insights into TMB-1 and the role of residue 119 and 228 in substrate and inhibitor binding

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.1
Synchrotron site	BESSY
Beamline	14.1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-05-11
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.918409
Spacegroup name	P 21 21 2
Unit cell lengths	71.398, 127.195, 44.274
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.287 - 1.750
R-factor	0.1951
Rwork	0.192
R-free	0.24790
RMSD bond length	0.012
RMSD bond angle	1.319
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.000	1.810
High resolution limit [Å]	1.750	1.750
Rmerge	0.082	0.492
Number of reflections	38067
<I/σ(I)>	10.8	1.7
Completeness [%]	91.9	59.25
Redundancy	3.8	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	295	0.10 M HEPES pH 8.0, 4.75% glycerol 32% polyethylene glycol (PEG) monomethyl ether (MME) 2k.