Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri

Author(s)

Souza, C. S. ; Ferreira, L. C. S. ; Thomas, L. ; Barbosa, J. A. R. G. ; Balan, A.

• Document type: Journal article
• Source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 65, p. 3-pg., 2009-02-01.

Abstract

Maltose-binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 Kusing the hanging-drop vapour-diffusion method. The crystal belonged to the primitive hexagonal space group P6(1)22, with unit-cell parameters a = 123.59, b = 123.59, c = 304.20 angstrom, and contained two molecules in the asymetric unit. It diffracted to 2.24 angstrom resolution. (AU)

• FAPESP's process: 01/07540-3 - Application of Associated Laboratory for the Structural Genomics Program
• Grantee: Luis Carlos de Souza Ferreira
• Support Opportunities: Regular Research Grants
• FAPESP's process: 00/10266-8 - A structural biology laboratory network for the study of the 3D structures of proteins
• Grantee: Nilson Ivo Tonin Zanchin
• Support Opportunities: Genome Research Grants