1UFH

Structure of putative acetyltransferase, YYCN protein of Bacillus subtilis

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 5ID-B
Synchrotron site	APS
Beamline	5ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2003-04-20
Detector	MARRESEARCH
Wavelength(s)	0.9792, 0.9565
Spacegroup name	C 1 2 1
Unit cell lengths	87.260, 88.580, 55.800
Unit cell angles	90.00, 98.80, 90.00

Refinement procedure

Resolution	26.080 - 2.200
R-factor	0.2339
Rwork	0.233
R-free	0.25900 *
Structure solution method	MAD
RMSD bond length	0.012
RMSD bond angle	1.260 *
Data scaling software	XDS
Phasing software	SHARP
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.080	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.085 *	0.238 *
Number of reflections	21192 *
<I/σ(I)>	6.8	18.8
Completeness [%]	99.3	99.3
Redundancy	3.8	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	22 *	900mM Ammonium phosphate, 190mM Sodium chloride, 100mM Imidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	ammonium phosphate	900 (mM)
3	1	reservoir		190 (mM)
4	1	reservoir	imidazole	100 (mM)	pH8.0