1PQA

Trypsin with PMSF at atomic resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	CCD
Collection date	2002-09-17
Detector	MARRESEARCH
Wavelength(s)	0.8110
Spacegroup name	P 1 21 1
Unit cell lengths	33.066, 66.763, 39.274
Unit cell angles	90.00, 108.02, 90.00

Refinement procedure

Resolution	25.000 - 1.230
Rwork	0.141
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000 *	1.240
High resolution limit [Å]	1.230	1.230
Rmerge	0.046 *
Number of reflections	44081 *
<I/σ(I)>	11	2.7
Completeness [%]	93.8	76.3
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5	293	Rypniewski, W.R., (1993) Protein Eng., 6, 341. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12.5 (mg/ml)
2	1	drop	ammonium sulfate	0.7 (M)
3	1	drop	citrate	50 (mM)
4	1	reservoir	ammonium sulfate	1.4 (M)
5	1	reservoir	sodium citrate	0.1 (M)