1N1M

Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1999-10-07
Detector	MARRESEARCH
Wavelength(s)	1.0266
Spacegroup name	P 21 21 21
Unit cell lengths	119.234, 123.448, 131.315
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.500
R-factor	0.211
Rwork	0.208
R-free	0.26100 *
Structure solution method	MAD
RMSD bond length	0.007 *
RMSD bond angle	1.600 *
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNX (2002)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.560
High resolution limit [Å]	2.500	2.500
Rmerge	0.071	0.352
Number of reflections	63399
<I/σ(I)>	15.5
Completeness [%]	93.7	64.8
Redundancy	9.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8	293	PEG4000, Sodium acetate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	Vapor diffusion, sitting drop *	8	293	PEG4000, Sodium acetate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	Vapor diffusion, sitting drop *	8	293	PEG4000, Sodium acetate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	40 (mg/ml)
2	1	drop	Tris	20 (mM)	pH8.0
3	1	drop		25 (mM)
4	1	reservoir	sodium acetate	0.3 (M)
5	1	reservoir	PEG4000	17-18 (%(w/v))
6	1	reservoir	Tris	0.1 (M)	pH8.0