Purification, crystallization and preliminary crystallographic analysis of the periplasmic binding protein ProX from Escherichia coli.
A periplasmic binding protein (ProX) for the compatible solutes glycine betaine and proline betaine from Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. Crystals were grown using a protein concentration of 10 mg ml(-1) and a precipitant of 26-28% PEG 4000 in 50 mM PIPES pH 6.2-6.4. Native diffraction data to 1.93 A resolution have been obtained from crystals at 290 K. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 48.1, b = 55.0, c = 115.7 A, and contain one molecule per asymmetric unit.
Breed J
Fachbereich Biologie, Universität Konstanz, 78457 Konstanz, Germany. jason.breed@astrazeneca.com
Kneip S
Gade J
Welte W
Bremer E
D001622:Betaine / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry; D011487:Protein Conformation
D002352:Carrier Proteins; D001622:Betaine; D011392:Proline; C003342:stachydrine