1NU6

Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	90
Detector technology	CCD
Collection date	2001-11-04
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9765
Spacegroup name	P 21 21 21
Unit cell lengths	65.496, 68.240, 419.289
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 2.100
R-factor	0.21747
Rwork	0.215
R-free	0.26500 *
Structure solution method	MAD
RMSD bond length	0.018
RMSD bond angle	1.860 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.000	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.084 *	0.268
Total number of observations	234528 *
Number of reflections	87113
Completeness [%]	82.9	72.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8.5	293	PEG, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG3350	20-25 (%)
3	1	reservoir		200 (mM)
4	1	reservoir	Tris		pH8.5
5	1	reservoir	glycerol	15 (%)