1OC9

TRYPAREDOXIN II FROM C.FASCICULATA solved by MR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2001-03-15
Detector	MARRESEARCH
Spacegroup name	P 41 21 2
Unit cell lengths	114.296, 114.296, 101.973
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.350
R-factor	0.19716
Rwork	0.196
R-free	0.21300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oc8
RMSD bond length	0.021 *
RMSD bond angle	1.650 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.390
High resolution limit [Å]	2.350	2.350
Rmerge	0.053	0.249
Total number of observations	136117 *
Number of reflections	28025
<I/σ(I)>	29.8	9.6
Completeness [%]	97.5	99.9
Redundancy	4.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	sodium citrate	500 (mM)
3	1	reservoir	HEPES	30 (mM)	pH7.5
4	1	reservoir	dithiothreitol	5 (mM)