4H86

Crystal structure of Ahp1 from Saccharomyces cerevisiae in reduced form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U
Synchrotron site	SSRF
Beamline	BL17U
Temperature [K]	100
Detector technology	CCD
Collection date	2011-11-08
Detector	RAYONIX MX-225
Wavelength(s)	0.97915
Spacegroup name	I 21 3
Unit cell lengths	149.049, 149.049, 149.049
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.131 - 2.004
R-factor	0.1584
Rwork	0.158
R-free	0.17340
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ENTRIES 1TP9 3uma 1NM3 AND 2PWJ
RMSD bond length	0.006
RMSD bond angle	0.907
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHENIX
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.030
High resolution limit [Å]	2.000	5.430	2.000
Rmerge	0.125	0.076	0.765
Number of reflections	37056
<I/σ(I)>	9
Completeness [%]	100.0	99.7	100
Redundancy	44.8	43.4	45

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.4	298	Protein Solution (40 mg/ml Ahp1 protein, in Milli-Q water containing 10mM DTT) mixed in a 1:1 ratio with the well solution (0.1 M BIS-TRIS pH 5.4, 2.0 M Ammonium Sulfate) Cryoprotected with 20% Glycerol , VAPOR DIFFUSION, HANGING DROP, temperature 298K