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X-ray Intensity Data (x-ray + intensity_data)
Selected AbstractsPreliminary X-ray diffraction studies of the external functional unit RtH2-e from the Rapana thomasianaACTA CRYSTALLOGRAPHICA SECTION D, Issue 11 2001M. Perbandt The `external' oxygenated functional unit RtH2-e of the Rapana hemocyanin subunit RHSS2 was isolated and crystallized. X-ray intensity data to 3.3,Å resolution have been collected at 100,K and the structure has been solved using the molecular-replacement method. The space group is assigned to be the tetragonal P43212, with unit-cell parameters a = b = 105.5, c = 375.0,Å. [source] Crystallization of the plant hormone receptors PYL9/RCAR1, PYL5/RCAR8 and PYR1/RCAR11 in the presence of (+)-abscisic acidACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2010Nobuyuki Shibata Abscisic acid (ABA) is a plant hormone that plays key regulatory roles in physiological pathways for the adaptation of vegetative tissues to abiotic stresses such as water stress in addition to events pertaining to plant growth and development. The Arabidopsis ABA receptor proteins PYR/PYLs/RCARs form a START family that contains 14 members which are classified into three subfamilies (I,III). Here, purification, crystallization and X-ray data collection are reported for a member of each of the subfamilies, PYL9/RCAR1 from subfamily I, PYL5/RCAR8 from subfamily II and PYR1/RCAR11 from subfamily III, in the presence of (+)-abscisic acid. The three proteins crystallize in space groups P3121/P3221, P2 and P1, respectively. X-ray intensity data were collected to 1.9,2.6,Å resolution. [source] Purification and preliminary X-ray crystallographic studies of ,-microseminoprotein from human seminal plasmaACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2009Vijay Kumar ,-Microseminoprotein (,-MSP) is a small cysteine-rich protein with a molecular mass of 10,kDa. It was first isolated from human seminal plasma and has subsequently been identified from several species. Comparison of the amino-acid sequences of ,-MSP proteins suggests that the protein is a rapidly evolving protein. The function of ,-MSP is poorly understood. Furthermore, no crystal structure has been reported of any ,-MSP; therefore, determination of the crystal structure of ,-MSP is the foremost task in order to understand the function of this protein completely. Here, the purification, crystallization and preliminary X-ray diffraction analysis of ,-MSP from human seminal plasma are described. The protein was purified using anion-exchange and size-exclusion chromatography and the purified protein was crystallized using 0.1,M ammonium sulfate, 0.1,M HEPES buffer pH 7.0 and 20%(w/v) PEG 3350. The crystals belonged to the tetragonal space group P4322 and contained three ,-MSP molecules in the asymmetric unit. X-ray intensity data were collected to 2.4,Å resolution. [source] Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric ,-lactamaseACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2009SeungBum Kim ,-Lactam antibiotics such as penicillins and cephalosporins have a four-atom ring as a common element in their structure. The ,-lactamases, which catalyze the inactivation of these antibiotics, are of great interest because of their high incidence in pathogenic bacteria. A novel oligomeric class C ,-lactamase (Est-Y29) from a metagenomic library was expressed, purified and crystallized. The recombinant protein was expressed in Escherichia coli with an N-terminal 6×His tag and purified to homogeneity. EstY-29 was crystallized and X-ray intensity data were collected to 1.49,Å resolution using synchrotron radiation. [source] | ||||||||||