1UOP

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLY-PHE-GLU-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	70.700, 99.300, 110.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 - 1.850
R-factor	0.158
Rwork	0.156
R-free	0.19400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h2z
RMSD bond length	0.008 *
RMSD bond angle	1.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	1.920
High resolution limit [Å]	1.850	1.850
Rmerge	0.076	0.406
Total number of observations	247702 *
Number of reflections	66292
<I/σ(I)>	14.6	2.5
Completeness [%]	98.7	97
Redundancy	3.7	3.7

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)