2B3X

Structure of an orthorhombic crystal form of human cytosolic aconitase (IRP1)

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2004-02-26
Detector	MARRESEARCH
Wavelength(s)	1.741, 1.739, 1.283
Spacegroup name	C 2 2 21
Unit cell lengths	75.352, 103.307, 225.957
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	113.230 - 2.540
Rwork	0.180
R-free	0.22500
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	1.230
Data reduction software	XDS
Data scaling software	XDS
Phasing software	SHARP
Refinement software	REFMAC (5.2.0003)

Data quality characteristics

	Overall
Low resolution limit [Å]	113.230
High resolution limit [Å]	2.540
Rmerge	0.079
Number of reflections	28614
<I/σ(I)>	11.1
Completeness [%]	94.6
Redundancy	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP		293	VAPOR DIFFUSION, HANGING DROP, temperature 293K