2H1S

Crystal Structure of a Glyoxylate/Hydroxypyruvate reductase from Homo sapiens

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2006-04-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97928
Spacegroup name	P 1 21 1
Unit cell lengths	75.996, 66.436, 148.774
Unit cell angles	90.00, 98.59, 90.00

Refinement procedure

Resolution	49.326 - 2.450
Rwork	0.207
R-free	0.26430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gdh 1WWK as a basis of 2-member ensemble
RMSD bond length	0.015
RMSD bond angle	1.590
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.326	80.000	2.510
High resolution limit [Å]	2.450	6.040	2.450
Rmerge	0.157	0.098	0.504
Number of reflections	50144
<I/σ(I)>	7.087		2.261
Completeness [%]	93.3	99.6	80.3
Redundancy	6.2	7.2	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.0003 M TCEP, 0.005 MES PH 6.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (12% PEG 3350, 0.10 M MOPS PH 7). Crystal was cryo-protected with 15% PEG 3350, 0.10 M PIPES PH 6.5 and a final concentration of 25% Ethylene glycol, vapor diffusion, hanging drop, temperature 293K