1PIN

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS

Experimental procedure

Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-03
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	49.000, 49.000, 137.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 1.350
R-factor	0.223
Rwork	0.223
R-free	0.26600
Structure solution method	RIGID BODY REFINEMENT USING MIRAS DERIVED STRUCTURE
RMSD bond length	0.008
RMSD bond angle	1.270 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.390
High resolution limit [Å]	1.350	1.350
Rmerge	0.053 *	0.592 *
Number of reflections	33672
<I/σ(I)>	18	2
Completeness [%]	95.5	69
Redundancy	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	4 *	PROTEIN WAS CRYSTALLIZED AT 4 DEGREES CELSIUS FROM 2.4 M (NH4)2SO4, 1% (V/V) PEG 400, 0.1 M NA-HEPES, PH 7.5. PRIOR TO DATA COLLECTION, THE CRYSTALS WERE TRANSFERRED TO SOLUTIONS OF 40 % (V/V) PEG 400, 0.1 M NA-HEPES, PH 7.5 CONTAINING 0.05 M ALANINE-PROLINE DIPEPTIDE., temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	ammonium sulfate	2.00-2.50 (M)
3	1	reservoir	HEPES/Na+	100 (mM)	pH7.5
4	1	reservoir	PEG400	1 (%(v/v))
5	1	reservoir	dithiothreitol	1 (mM)