3O48

Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	CCD
Collection date	2009-10-19
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0
Spacegroup name	P 43 21 2
Unit cell lengths	46.020, 46.020, 139.220
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.740 - 1.750
R-factor	0.16635
Rwork	0.165
R-free	0.18788
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pqn
RMSD bond length	0.007
RMSD bond angle	0.853
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	BALBES
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	5.000	1.800
High resolution limit [Å]	1.750	4.000	1.750
Rmerge	0.324	0.310	0.510
Number of reflections	15603
<I/σ(I)>	10.21	11.95	6.84
Completeness [%]	95.8
Redundancy	23.26	21.73	26.16

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4	298	20% PEG 8000, 0.2M ammonium sulfate, 0.05 M Tris, 0.05 M NaCl, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K