4P6Y

Crystal structure of the M42 aminopeptidase TmPep1050 from Thermotoga maritima

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2013-04-27
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9797
Spacegroup name	P 1
Unit cell lengths	114.260, 114.570, 114.040
Unit cell angles	114.46, 91.71, 105.69

Refinement procedure

Resolution	44.045 - 2.200
R-factor	0.2136
Rwork	0.212
R-free	0.24740
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ylo
RMSD bond length	0.009
RMSD bond angle	1.254
Refinement software	PHENIX ((phenix.refine: dev_1539))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.050	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.089	0.392
Number of reflections	237152
<I/σ(I)>	8.56	2.22
Completeness [%]	93.5	84.76
Redundancy	3.2	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.75	292	TmPep1050 (390 uM) in 50 mM MOPS pH 7.2 with 0.5 M ammonium sulfate and 1 mM cobalt chloride, was mixed 2:2 with well buffer (2.1M malic acid pH 6.75) with 500 uL well buffer in the well of the crystallization tray