4MVA

1.43 Angstrom Resolution Crystal Structure of Triosephosphate Isomerase (tpiA) from Escherichia coli in Complex with Acetyl Phosphate.

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	2013-03-03
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	46.535, 67.529, 150.336
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.240 - 1.430
R-factor	0.13567
Rwork	0.135
R-free	0.15614
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tre
RMSD bond length	0.010
RMSD bond angle	1.471
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0046)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.450
High resolution limit [Å]	1.430	1.430
Rmerge	0.062	0.534
Number of reflections	88659
<I/σ(I)>	22.7	3.4
Completeness [%]	99.9	100
Redundancy	6.1	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	295	Protein: 7.4mg/mL, 0.15M Sodium cloride, 0.01M Tris-HCl pH 8.3; Screen: Classics II (F11), 0.2M Sodium chloride, 0.1M Bis-Tris pH 6.5, 25% (w/v) PEG 3350, 10mM ACP, VAPOR DIFFUSION, SITTING DROP, temperature 295K