1ML1

PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-12
Detector	MARRESEARCH
Spacegroup name	P 3
Unit cell lengths	165.230, 165.230, 51.230
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	32.000 - 2.600
R-factor	0.231
Rwork	0.231
R-free	0.24700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ttj
RMSD bond length	0.010
RMSD bond angle	1.610
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	21.000	2.640
High resolution limit [Å]	2.600	2.600
Rmerge	0.072	0.297 *
Total number of observations	124266 *
Number of reflections	45363
<I/σ(I)>	12	3
Completeness [%]	94.6	96.2
Redundancy	2.7	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	20 *	PLEASE SEE JRNL ARTICLE, pH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
10	1	reservoir		1.0 (M)
11	1	reservoir	ammonium sulphate	0.7 (M)
12	1	reservoir	dithiothreitol	1 (mM)
13	1	reservoir	EDTA	1 (mM)
14	1	reservoir	sodium azide	1 (mM)
2	1	drop	TEA-HCl	10 (mM)
3	1	drop		25 (mM)
4	1	drop	dithiothreitol	1 (mM)
5	1	drop	EDTA	1 (mM)
6	1	drop	sodium azide	1 (mM)
7	1	drop	2PG	10 (mM)
8	1	drop	reservoir solution		1 ml
9	1	reservoir	Tris-HCl	100 (mM)