2JLM

Structure of a Putative Acetyltransferase (ACIAD1637) from Acinetobacter baylyi ADP1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX10.1
Synchrotron site	SRS
Beamline	PX10.1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-02-24
Detector	MARRESEARCH
Spacegroup name	P 32
Unit cell lengths	78.410, 78.410, 197.760
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	68.000 - 2.350
Rwork	0.182
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2j8m
RMSD bond length	0.006
RMSD bond angle	1.029
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	68.000	2.410
High resolution limit [Å]	2.350	2.350
Rmerge	0.090	0.250
Number of reflections	56442
<I/σ(I)>	17.5	4
Completeness [%]	99.6	94.7
Redundancy	5.4	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5		CRYSTALS WERE GROWN USING HANGING DROP VAPOR DIFFUSION. RESERVOIR CONTAINED 500 MICROLITRES OF 0.1M TRIS-HCL AT PH6.5, 1.2M SODIUM ACETATE AND 0.1% SODIUM AZIDE. DROPS CONTAINED 1 MICROLITRE OF PROTEIN AT A CONCENTRATION OF 8MG/ML TO WHICH AN EQUAL VOLUME OF RESERVOIR WAS ADDED.