9H5W

X-ray structure of Hydrogenosomal processing peptidase (HPP), E56Q inactive mutant, from Trichomonas vaginalis co-crystallized with presequence peptide from adenylate kinase (AK) - not visible in the structure model

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	90
Detector technology	CCD
Collection date	2014-03-26
Detector	RAYONIX MX-225
Wavelength(s)	0.918
Spacegroup name	P 21 21 21
Unit cell lengths	87.788, 114.442, 124.633
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.000 - 2.000
R-factor	0.20227
Rwork	0.201
R-free	0.22853
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.013
RMSD bond angle	1.593
Data reduction software	XDS
Data scaling software	Aimless
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.000	2.040
High resolution limit [Å]	2.000	2.000
Rmerge	0.126	1.859
Rmeas	0.141	2.072
Rpim	0.062	0.903
Total number of observations		22339
Number of reflections	85304	4465
<I/σ(I)>	11.8	1
Completeness [%]	99.9
Redundancy	5	5
CC(1/2)	0.997	0.327

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	291	substrate co-crystallized MLSTLAKRF/ASGKKDRM 0.1 M MES buffer [pH 5.0], 2.4 M ammonium sulfate, 0.2 mM n-dodecylmaltoside