1GXT

Hydrogenase Maturation Protein HypF "acylphosphatase-like" N-terminal domain (HypF-ACP) in complex with Sulfate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Spacegroup name	H 3 2
Unit cell lengths	58.095, 58.095, 155.645
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 1.300 *
R-factor	0.136
Rwork	0.134
R-free	0.17170 *
Structure solution method	SIRAS
RMSD bond length	0.018 *
RMSD bond angle	1.746 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	autoSHARP
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	1.300
Rmerge	0.057
Total number of observations	299640 *
Number of reflections	28517
<I/σ(I)>	16.3
Completeness [%]	92.9
Redundancy	10.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5.5 *		pH 8.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	30.0 (%(w/v))
2	1	reservoir	sodium acetate	100 (mM)	pH5.5
3	1	drop	protein	8.0 (mg/ml)
4	1	drop	glycerol	10.0 (%(v/v))