title: Purification, crystallization and preliminary X-ray analysis of apo glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252).
abstract: Glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252) has been purified to homogeneity in the apo form. The protein was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a = 69.95, b = 93.68, c = 89.05 A, beta = 106.84 degrees . X-ray diffraction data have been collected and processed to a maximum resolution of 2.2 A. The presence of one tetramer in the asymmetric unit gives a Matthews coefficient (V(M)) of 1.81 A(3) Da(-1) with a solvent content of 32%. The structure has been solved by molecular replacement and structure refinement is now in progress.
authors.affiliation: Department of Biotechnology, Indian Institute of Technology, Kharagpur 721 302, India.
authors.forename: Somnath
authors.initials: S
authors.lastname: Mukherjee
authors.forename: Baisakhee
authors.initials: B
authors.lastname: Saha
authors.forename: Debajyoti
authors.initials: D
authors.lastname: Dutta
authors.forename: Amit Kumar
authors.initials: AK
authors.lastname: Das
mesh_terms: D001051:Apoenzymes / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000302:isolation & purification; D055624:Methicillin-Resistant Staphylococcus aureus / Q000201:enzymology*
chemical_list: D001051:Apoenzymes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
references.citation: J Biol Chem. 1975 Dec 10;250(23):9137-62
references.pmid: 127793
references.citation: Anal Biochem. 1976 May 7;72:248-54
references.pmid: 942051
references.citation: Infect Immun. 1999 Mar;67(3):1086-92
references.pmid: 10024547
references.citation: J Bacteriol. 1997 Aug;179(16):4992-9
references.pmid: 9260938
references.citation: Eur J Biochem. 1996 Feb 1;235(3):641-7
references.pmid: 8654412
references.citation: Biochemistry. 1999 Dec 7;38(49):16084-91
references.pmid: 10587431
references.citation: Acta Crystallogr D Biol Crystallogr. 1999 Oct;55(Pt 10):1718-25
references.pmid: 10531521
references.citation: Infect Immun. 1998 May;66(5):2052-9
references.pmid: 9573088
references.citation: J Exp Med. 1992 Aug 1;176(2):415-26
references.pmid: 1500854
references.citation: Biochemistry. 1963 May-Jun;2:512-8
references.pmid: 14069539
references.citation: Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt 10):929-32
references.pmid: 18931438
references.citation: Virology. 1998 Aug 15;248(1):46-52
references.pmid: 9705254
references.citation: J Mol Biol. 1968 Apr 28;33(2):491-7
references.pmid: 5700707
references.citation: Mol Microbiol. 2002 Mar;43(6):1603-14
references.pmid: 11952908
references.citation: J Biol Chem. 1953 Sep;204(1):265-81
references.pmid: 13084599
references.citation: Microbiology (Reading). 2001 Feb;147(Pt 2):411-417
references.pmid: 11158358
references.citation: Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
references.pmid: 15299926
references.citation: Biochem J. 1971 Mar;122(1):59-69
references.pmid: 4330968
references.citation: Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):449-57
references.pmid: 15805600
references.citation: Arch Biochem Biophys. 1999 Mar 15;363(2):259-66
references.pmid: 10068447
references.citation: Biochemistry. 1989 Mar 21;28(6):2586-92
references.pmid: 2659073
references.citation: Biochim Biophys Acta. 1999 Jul 13;1432(2):159-84
references.pmid: 10407139