TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture
AU - Dias, João Miguel L.
AU - Carvalho, A. L.
AU - Kölln, Ingo
AU - Calvete, Juan J.
AU - Töpfer-Petersen, Edda
AU - Varela, Paloma Fernández
AU - Romero, Antonio
AU - Urbanke, Claus
AU - Romão, M J
PY - 1997
Y1 - 1997
N2 - Bovine acidic seminal fluid protein (aSFP) is a 1.29 kDa polypeptide of the spermadhesin family built by a single CUB domain architecture. The CUB domain is an extracellular module present in 16 functionally diverse proteins. To determine the three-dimensional structure of aSFP, the protein was crystallized at 21 degrees C by vapor diffusion in hanging drops, using ammonium sulfate, pH 4.7, and polyethyleneglycol 4,000 as precipitants, containing 10% dioxane to avoid the formation of clustered crystals. Elongated prismatic crystals with maximal size of 0.6 x 0.3 x 0.2 mm3 diffract to beyond 1.9 A resolution and belong to space group P2(1)2(1)2(1), with cell parameters a = 52.4 A, b = 41.5 A, c = 48.2 A. There is one aSFP molecule per asymmetric unit, which corresponds to a crystal volume per unit molecular mass of 2.04 A3/Da, and analytical ultracentrifugation analysis show that aSFP is a monomeric protein.
AB - Bovine acidic seminal fluid protein (aSFP) is a 1.29 kDa polypeptide of the spermadhesin family built by a single CUB domain architecture. The CUB domain is an extracellular module present in 16 functionally diverse proteins. To determine the three-dimensional structure of aSFP, the protein was crystallized at 21 degrees C by vapor diffusion in hanging drops, using ammonium sulfate, pH 4.7, and polyethyleneglycol 4,000 as precipitants, containing 10% dioxane to avoid the formation of clustered crystals. Elongated prismatic crystals with maximal size of 0.6 x 0.3 x 0.2 mm3 diffract to beyond 1.9 A resolution and belong to space group P2(1)2(1)2(1), with cell parameters a = 52.4 A, b = 41.5 A, c = 48.2 A. There is one aSFP molecule per asymmetric unit, which corresponds to a crystal volume per unit molecular mass of 2.04 A3/Da, and analytical ultracentrifugation analysis show that aSFP is a monomeric protein.
KW - acidic seminal fluid protein
KW - analytical ultracentrifugation
KW - aSFP
KW - bovine seminal plasma
KW - crystallization
KW - CUB domain
KW - spermadhesin protein family
KW - X-ray diffraction analysis
U2 - 10.1002/pro.5560060323
DO - 10.1002/pro.5560060323
M3 - Article
C2 - 9070456
VL - 6
SP - 725
EP - 727
JO - Protein Science
JF - Protein Science
SN - 0961-8368
IS - 3
ER -