1ITU

HUMAN RENAL DIPEPTIDASE COMPLEXED WITH CILASTATIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1996-11-30
Detector	RIGAKU
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	80.179, 79.491, 56.951
Unit cell angles	90.00, 96.34, 90.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.1898
Rwork	0.185
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NATIVE DIPEPTIDASE STRUCTURE
RMSD bond length	0.007
RMSD bond angle	22.760 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.087	0.274
Total number of observations	185396 *
Number of reflections	46290
<I/σ(I)>	13.4
Completeness [%]	96.1	84.5
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6 *	10 *	Nitanai, Y., (1996) J.CRYST.GROWTH, 168, 280. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	PEG8000	7.5 (%(w/v))	pH5.6
3	1	reservoir	PEG8000	15 (%)	pH5.6