1UOQ

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX14.1
Synchrotron site	SRS
Beamline	PX14.1
Temperature [K]	100
Detector technology	CCD
Collection date	2003-05-09
Detector	ADSC CCD
Spacegroup name	P 21 21 21
Unit cell lengths	70.300, 99.100, 109.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.000 - 2.100
R-factor	0.149
Rwork	0.147
R-free	0.20500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h2z
RMSD bond length	0.026 *
RMSD bond angle	1.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.089	0.129
Total number of observations	153386 *
Number of reflections	43221
<I/σ(I)>	13.8	3.7
Completeness [%]	95.1	76.8
Redundancy	3.5	2.1

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)