1FNO

PEPTIDASE T (TRIPEPTIDASE)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	1999-09-30
Detector	ADSC
Spacegroup name	C 1 2 1
Unit cell lengths	132.374, 46.036, 96.591
Unit cell angles	90.00, 116.11, 90.00

Refinement procedure

Resolution	500.000 - 2.400
R-factor	0.224 *
Rwork	0.222
R-free	0.26200 *
RMSD bond length	0.011
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.046	0.246
Total number of observations	99755 *
Number of reflections	20598
<I/σ(I)>	23.4
Completeness [%]	99.2	99.2
Redundancy	4.8	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	293	Hakansson, K., (2000) Acta Crystallogr., Sect.D, 56, 924. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium potassium tartrate		or ammonium sulfate
2	1	reservoir	Bis-Tris		or Tris