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Publication Abstract from PubMed
The peptidoglycan-associated lipoprotein (Pal) from Escherichia coli is part of the Tol--Pal multiprotein complex used by group A colicins to penetrate and kill cells. Pal homologues are found in many Gram-negative bacteria and the Tol--Pal system is thought to play a role in bacterial envelope integrity. The Pal protein comprises 152 amino acids. Crystals of the C-terminal 109-amino-acid fragment of the Pal protein have been produced. The crystals belong to the tetragonal space group I4(1), with unit-cell parameters a = b = 89.3, c = 67.2 A. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 A resolution using synchrotron radiation. Selenomethionine-substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.
Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.,Abergel C, Walburger A, Chenivesse S, Lazdunski C Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. PMID:11173492[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Abergel C, Walburger A, Chenivesse S, Lazdunski C. Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. PMID:11173492
