1EXC

CRYSTAL STRUCTURE OF B. SUBTILIS MAF PROTEIN COMPLEXED WITH D-(UTP)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS
Synchrotron site	APS
Temperature [K]	100
Detector technology	CCD
Collection date	1999-09-01
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	62.100, 86.580, 93.730
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	17.000 - 2.700
Rwork	0.197
R-free	0.26000
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.137	0.287
Number of reflections	12658
<I/σ(I)>	15.5
Completeness [%]	89.2	92
Redundancy	4.4	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	295	drop consists of equal volume of protein and reservoir solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	Tris-HCl	0.1 (M)
3	1	reservoir	PEG8000	8 (%)