1Q40

Crystal structure of the C. albicans Mtr2-Mex67 M domain complex

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	100
Detector technology	CCD
Collection date	2003-01-24
Detector	MARRESEARCH
Wavelength(s)	0.9881,0.9809,0.815
Spacegroup name	P 1 21 1
Unit cell lengths	70.414, 54.077, 109.751
Unit cell angles	90.00, 96.12, 90.00

Refinement procedure

Resolution	12.000 - 1.950
R-factor	0.17775
Rwork	0.177
R-free	0.22600 *
Structure solution method	MAD
RMSD bond length	0.010 *
RMSD bond angle	1.190 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.000
High resolution limit [Å]	1.950	1.950
Rmerge	0.053 *	0.311 *
Total number of observations	530670 *
Number of reflections	56333 *
<I/σ(I)>	9.5	2.3
Completeness [%]	91.6	67
Redundancy	4.3	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6	20 *	PEG 4000, imidazol-malate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	18 (%)
2	1	reservoir	imidazole-malate	0.2 (M)	pH6.0
3	1	drop	protein	9.5 (mg/ml)