4K6A

Revised Crystal Structure of apo-form of Triosephosphate Isomerase (tpiA) from Escherichia coli at 1.8 Angstrom Resolution.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2013-03-15
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.03326
Spacegroup name	P 21 21 21
Unit cell lengths	46.066, 67.488, 149.769
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.060 - 1.800
R-factor	0.15075
Rwork	0.149
R-free	0.18470
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tre
RMSD bond length	0.012
RMSD bond angle	1.327
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	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.088	0.529
Number of reflections	44231
<I/σ(I)>	18.3	2.6
Completeness [%]	99.9	98.4
Redundancy	5.8	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	295	Protein: 7.6mg/mL, 0.5M Sodium cloride, 0.01M Tris-HCl pH 8.3; Screen: PACT (D11), 0.2M Calcium chloride, 0.1M Tris-HCl pH 8.0, 20% (w/v) PEG 6000., VAPOR DIFFUSION, SITTING DROP, temperature 295K