3G87

Crystal structure of malonyl CoA-acyl carrier protein transacylase from Burkholderia pseudomallei using dried seaweed as nucleant or protease

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2009-02-05
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54180
Spacegroup name	P 21 21 21
Unit cell lengths	57.495, 69.196, 83.202
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.300
R-factor	0.212
Rwork	0.210
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mla
RMSD bond length	0.019
RMSD bond angle	1.740
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.380
High resolution limit [Å]	2.300	4.950	2.300
Rmerge	0.151	0.096	0.498
Number of reflections	14632
<I/σ(I)>	9.025
Completeness [%]	95.4	87.4	99.2
Redundancy	4.7	4.6	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	24.5 mg/mL protein, JCSG+ screen well h6; used dried seaweed as nucleant or protease as described by Thakur et al PLOS one 2007, 2, e1091 and D'Arcy et al Acta Cryst D 2003, 59, 1343; 0.1 M BisTris pH 5.5, 17% PEG 10,000, 0.1 M NH4OAC; Crystal ID 201868h6, VAPOR DIFFUSION, SITTING DROP, temperature 289K