1UW1

A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-15
Detector	MARRESEARCH
Spacegroup name	P 32 2 1
Unit cell lengths	71.077, 71.077, 54.883
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 1.940
R-factor	0.199 *
Rwork	0.200
R-free	0.22840 *
Structure solution method	MAD
RMSD bond length	0.018
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXD
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.000
High resolution limit [Å]	1.940	1.940
Rmerge	0.069	0.477
Total number of observations	108633 *
Number of reflections	12124
<I/σ(I)>	32	7.3
Completeness [%]	99.5	99.3
Redundancy	9	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5 *		USING THE HANGING-DROP VAPOR DIFFUSION TECHIQUE. 20MG/ML OF PROTEIN WAS MIXED IN EQUAL VOLUMES WITH A CRYSTALLIZATION BUFFER OF 0.1M TRIS/HCL PH 8.5, 0.2 M SODIUM CITRATE, 30% PEG 400)

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	add	protein	20 (mg/ml)
2	1	reservoir	Tris-HCl	0.1 (M)
3	1	reservoir	sodium citrate	0.2 (M)
4	1	reservoir	PEG400	30 (%)