1UOO

Prolyl oligopeptidase from porcine brain, S554A mutant with bound peptide ligand GLY-PHE-ARG-PRO

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-02-11
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	70.200, 98.700, 109.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.000 - 2.350
R-factor	0.195
Rwork	0.193
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h2z
RMSD bond length	0.006 *
RMSD bond angle	0.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	51.000	2.430
High resolution limit [Å]	2.350	2.350
Rmerge	0.099	0.467
Total number of observations	117435 *
Number of reflections	31460
<I/σ(I)>	12.6	2.2
Completeness [%]	97.6 *	98.7
Redundancy	3.9	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	4 *	Fulop, V., (1998) Cell(Cambridge,Mass.), 94, 161. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	mPEG5000	17 (%(w/v))
2	1	reservoir	glycerol	15 (%(v/v))
3	1	reservoir	monothioglycerol	1 (%(v/v))
4	1	reservoir		20 (mM)
5	1	reservoir	Tris	100 (mM)
6	1	drop	protein	10 (mg/ml)