4ECM

2.3 Angstrom Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase from Bacillus anthracis in Complex with Thymidine-5-diphospho-alpha-D-glucose and Pyrophosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2012-03-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 6 2 2
Unit cell lengths	135.072, 135.072, 85.138
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.240 - 2.300
R-factor	0.15442
Rwork	0.153
R-free	0.18588
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3hl3
RMSD bond length	0.011
RMSD bond angle	1.526
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.108	0.533
Number of reflections	20938
<I/σ(I)>	22.9	5.1
Completeness [%]	99.9	100
Redundancy	10.7	10.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	295	Protein: 7.5 mg/mL, 0.5M NaCl, 0.01M Tris-HCl (pH 8.3), 0.001M Thymidine-5-diphospho-alpha-D-glucose. Screen: PACT (H8), 0.2 Sodium Sulfate, 0.1M TRIS propane, 20% (w/v) PEG 33500, VAPOR DIFFUSION, SITTING DROP, temperature 295K