TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of β-amylase from Bacillus polymyxa
AU - Yamane, Takashi
AU - Tasaki, Hiroshi
AU - Matsumoto, Fusako
AU - Suzuki, Atsuo
AU - Uozumi, Nobuyuki
AU - Ashida, Tamaichi
PY - 1999/4
Y1 - 1999/4
N2 - A truncated β-amylase (E.C. 3.2.1.2) from Bacillus polymyxa has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals belong to the orthorhombic space group P212121 with cell dimensions a = 64.6, b = 141.9, c = 155.1 Å and diffract to 2.5 Å resolution. The asymmetric unit containing three protein molecules was derived from an electron-density map calculated at 4 Å resolution using MIR phases. This gives a V(m) value of 2.36 Å3 Da-1.
AB - A truncated β-amylase (E.C. 3.2.1.2) from Bacillus polymyxa has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals belong to the orthorhombic space group P212121 with cell dimensions a = 64.6, b = 141.9, c = 155.1 Å and diffract to 2.5 Å resolution. The asymmetric unit containing three protein molecules was derived from an electron-density map calculated at 4 Å resolution using MIR phases. This gives a V(m) value of 2.36 Å3 Da-1.
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U2 - 10.1107/S0907444998017570
DO - 10.1107/S0907444998017570
M3 - Article
C2 - 10089328
AN - SCOPUS:0033118680
SN - 0907-4449
VL - 55
SP - 898
EP - 900
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
IS - 4
ER -