4BI7

CRYSTAL STRUCTURE OF A MUTANT (C202A) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

Replaces:  2YC7

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	90
Detector technology	CCD
Collection date	2010-07-28
Detector	MARRESEARCH
Spacegroup name	I 2 2 2
Unit cell lengths	55.548, 102.021, 118.769
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.690 - 1.600
R-factor	0.18139
Rwork	0.180
R-free	0.19817
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2dp3
RMSD bond length	0.009
RMSD bond angle	1.217
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	PHASER (FOR MR)
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.700	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.060	0.270
Number of reflections	44874
<I/σ(I)>	12.9	4
Completeness [%]	99.3	99.3
Redundancy	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.5		PROTEIN WAS CRYSTALLYZED FROM 0.1 M MES MONOHYDRATE PH 6.5, 12 % W/V POLYETHYLENE GLYCOL 20,000