Table 1

Data collection and refinement. Expression, purification, and crystallization of FGFR1K were done as described (22). Crystals of native FGFR1K (space group C2, two molecules in the asymmetric unit) were soaked in 500 μl of stabilizing solution [25% PEG 10000, 0.3 M (NH4)2SO4, 0.1 M bis-tris (pH 6.5), and 5% ethylene glycol] containing SU4984 (5 mM) or SU5402 (1 mM) at 4°C for 24 to 48 hours. Data were collected on a Rigaku RU-200 rotating anode (Cu Kα) operating at 50 kV and 100 mA and equipped with double-focusing mirrors and an R-AXIS IIC image plate detector. One cryo-cooled crystal was used for each data set. Crystals were flash-cooled in a dry nitrogen stream at −175°C. Data were processed with DENZO and SCALEPACK (36). Difference Fourier electron density maps were computed using phases calculated from the structure of unliganded FGFR1K (22). X-PLOR (37) was used for simulated annealing (1000 K) and conjugate-gradient minimization, and TOM/FRODO (38) was used for model building. The average B factor for all atoms is 38.3 Å2 for FGFR1K-SU4984 and 39.2 Å2 for FGFR1K-SU5402.

ParameterSU4984SU5402
Data collection statistics
Resolution (Å) 20.0–2.4 20.0–2.5
Observations (n)94093 93535
Completeness (%)* 99.1 (97.9) 97.6 (96.1)
Redundancy3.3 3.7
R s y m (%)* 6.3 (32.2) 6.8 (23.0)
Signal 〈I > σI〉11.4 11.8
Refinement statistics
Resolution (Å) 6.0–2.4 6.0–2.5
Reflections (n) 2353020402
R value (%)§ | 19.5 (28.1) 19.0 (27.0)
Bonds (Å) 0.008 0.008
Angles (°) 1.3 1.4
B factors (Å2) # 1.5 1.5
  • * Value in parentheses is for the highest resolution shell.

  • R sym = 100 × ΣhklΣi |Ii(hkl) − 〈I(hkl)〉|/ΣhklΣiIi(hkl).

  • For FGFR1K-SU4984: 550 residues, 234 water molecules, 2 SU4984 molecules (4608 atoms); for FGFR1K-SU5402: 550 residues, 229 water molecules, 2 SU5402 molecules (4636 atoms).

  • § R value = 100 × ΣhklF o(hkl)| − |F c(hkl)∥/Σhkl|F o(hkl)|, where F o and F c are the observed and calculated structure factors, respectively (F o > 2σ).

  • | Value in parentheses is the free R value determined from 5% of the data.

  • Root-mean-square deviation.

  • # For bonded protein atoms.