1FCH

CRYSTAL STRUCTURE OF THE PTS1 COMPLEXED TO THE TPR REGION OF HUMAN PEX5

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	93
Detector technology	IMAGE PLATE
Collection date	2000-05-09
Detector	RIGAKU RAXIS II
Spacegroup name	C 1 2 1
Unit cell lengths	137.960, 73.510, 87.560
Unit cell angles	90.00, 120.78, 90.00

Refinement procedure

Resolution	29.630 - 2.200
R-factor	0.194
Rwork	0.194
R-free	0.22400
RMSD bond length	0.006
RMSD bond angle	18.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.240
High resolution limit [Å]	2.200	2.200
Rmerge	0.055	0.227
Number of reflections	38298
<I/σ(I)>	21.8
Completeness [%]	99.8	98.8
Redundancy	3.6	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	peptide solution was diluted 1:1 with reservoir *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	0.24 (mM)
2	1	drop		50 (mM)
3	1	drop	HEPES	5 (mM)
4	1	drop	peptide	1.9 (mM)
5	1	reservoir	Na citrate	0.58 (M)
6	1	reservoir	HEPES	0.1 (M)