1E2Y

Tryparedoxin peroxidase from Crithidia fasciculata

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	1999-06-15
Detector	MARRESEARCH
Wavelength(s)	0.8800,0.9790,0.9792
Spacegroup name	P 1 21 1
Unit cell lengths	123.800, 97.200, 133.800
Unit cell angles	90.00, 93.10, 90.00

Refinement procedure

Resolution	21.000 - 3.200
R-factor	0.273
Rwork	0.273
R-free	0.28600
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	23.410 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	21.000	21.000
High resolution limit [Å]	3.200	3.200
Rmerge	0.091 *	0.480 *
Total number of observations	376643 *
Number of reflections	52094
<I/σ(I)>	14.8	2.6
Completeness [%]	99.8	96.7
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5		drop consists of 2.5 micro litter of protein mixed with 2 micro litter of reservoir solution and 0.5 micro litter EDTA *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	16 (mg/ml)
2	1	drop	EDTA	0.1 (M)
3	1	reservoir	PEG1000	12.5 (%(w/v))
4	1	reservoir	Tris-HCl	100 (mM)
5	1	reservoir	glycerol	10 (%(v/v))
6	1	reservoir	dithiothreitol	100 (mM)
7	1	reservoir	DMSO	0.25 (%(v/v))