1N8N

Crystal structure of the Au3+ complex of AphA class B acid phosphatase/phosphotransferase from E. coli at 1.69 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2002-07-13
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0377, 1.0404, 0.9392
Spacegroup name	I 2 2 2
Unit cell lengths	49.279, 92.457, 138.182
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 * - 1.690
R-factor	0.17906
Rwork	0.178
R-free	0.20700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MAD-phased Bromine derivative at 2.2 A resolution
RMSD bond length	0.020 *
RMSD bond angle	1.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000 *	1.790
High resolution limit [Å]	1.690	1.690
Rmerge	0.075 *	0.375 *
Total number of observations	135549 *
Number of reflections	31884	2579 *
<I/σ(I)>	7	7
Completeness [%]	98.2 *	92 *
Redundancy	4.3 *	2.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	293	AphA 6mg/mL, 50 mM Na acetate, 25% PEG 6000, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K. The crystals of the native enzyme (containing Mg2+ or Zn2+) have been soaked in 1 mM solution of AuCl3

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG6000	17-22 (%)
3	1	reservoir		1 (mM)